|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-252 |
6.02e-78 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 235.71 E-value: 6.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFL 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSL-PPGEVTALLGPNGSGKSTLLRALAGLLKPSsGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 PQSLPQGVHLHVLEsiiVVL------RASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpe 156
Cdd:COG1120 81 PQEPPAPFGLTVRE---LVAlgryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEpp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 157 lllldeplSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRV 236
Cdd:COG1120 158 lllldeptSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGV 237
|
250
....*....|....*.
gi 1167959503 237 RGRVERCSQGKLQVVL 252
Cdd:COG1120 238 EARVIEDPVTGRPLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-219 |
4.49e-54 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 172.62 E-value: 4.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQ 84
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSI-EAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 slpqgvhlhvlesiivvlrasggrdnaqgraqilaILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 165 SALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-242 |
2.43e-51 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 167.88 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKVVFL 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSL-PTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 PQslpqgvHLHVLESIIVV-LRASG--------GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIR 153
Cdd:PRK11231 82 PQ------HHLTPEGITVReLVAYGrspwlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEV 233
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
....*....
gi 1167959503 234 YRVRGRVER 242
Cdd:PRK11231 235 FDVEAEIHP 243
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-252 |
6.06e-49 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 161.82 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 5 MLRSFSAGYSTQ--PVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVF 81
Cdd:COG4559 1 MLEAENLSVRLGgrTLLDDVSLTLRP-GELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSLPQGVHLHVLEsiiVVL--RASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSL--IRRPEL 157
Cdd:COG4559 80 LPQHSSLAFPFTVEE---VVAlgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 158 LLLDEP-----LSALDLNYQFHVMDLVRRDTQARNRVtIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAE 232
Cdd:COG4559 157 GGPRWLfldepTSALDLAHQHAVLRLARQLARRGGGV-VAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250 260
....*....|....*....|
gi 1167959503 233 VYRVRGRVERCSQGKLQVVL 252
Cdd:COG4559 236 VYGADLRVLAHPEGGCPQVL 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-240 |
1.92e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.00 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVL 95
Cdd:PRK13548 16 TLLDDVSLTLRP-GEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 EsiiVVL--RASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP------LSAL 167
Cdd:PRK13548 95 E---VVAmgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPPRWllldepTSAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 168 DLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRGRV 240
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLV 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-248 |
1.55e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 147.92 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVH 91
Cdd:COG4604 11 YGGKVVLDDVSLTI-PKGGITALIGPNGAGKSTLLSMISRLLPPDsGEVLVDGLDVATTPSRELAKRLAILRQENHINSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLEsiivvLRA------SGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:COG4604 90 LTVRE-----LVAfgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 166 ALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRGRVERCSQ 245
Cdd:COG4604 165 NLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVEEIDG 244
|
...
gi 1167959503 246 GKL 248
Cdd:COG4604 245 KRI 247
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-237 |
4.67e-36 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 128.95 E-value: 4.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSL 86
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEI-PDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQGVHLHVLEsiivvLRASG--------GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:PRK10253 91 TTPGDITVQE-----LVARGryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 159 LLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVR 237
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLR 244
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-240 |
1.23e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmslsfAERAQKVVFLPQ 84
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTI-PPGEFVAIVGPNGAGKSTLLKAILGLLPPTsGTVRLFGKPP-----RRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 --SLPQGVHLHVLEsiiVVL----RASG--GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPE 156
Cdd:COG1121 83 raEVDWDFPITVRD---VVLmgryGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 157 LLLLDEPLSALDLNYQFHVMDLVRRdtQARNRVTI-VVAHDINIALRHGDHVLMLkDGRLVASGAPETVITAERLAEVYR 235
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRE--LRREGKTIlVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYG 236
|
....*
gi 1167959503 236 VRGRV 240
Cdd:COG1121 237 GPVAL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-242 |
2.87e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 128.87 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD----GEALLDGEDLMSLSFAERAQK 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLtIAPGETVALVGESGSGKSTLALALMGLLPHGgrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFLPQS-LPQGVHLHVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPEL 157
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 158 LLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA-ERLAEVYRV 236
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApQALAAVPRL 243
|
....*.
gi 1167959503 237 RGRVER 242
Cdd:COG1123 244 GAARGR 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-234 |
4.93e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 122.68 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLS-FAERAQ--KVVFLPQSLPQGVHLHVLESIIV--- 100
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEPTsGSVLIDGTDINKLKgKALRQLrrQIGMIFQQFNLIERLSVLENVLSgrl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 ----VLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVM 176
Cdd:cd03256 105 grrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 177 DLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETvITAERLAEVY 234
Cdd:cd03256 185 DLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
5.85e-34 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 121.86 E-value: 5.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFl 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTV-EPGEFLALLGPSGCGKTTLLRLIAGLERPDsGEILIDGRDVTGVPPERRNIGMVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 pQSLPQGVHLHVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:cd03259 79 -QDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 163 PLSALDLNYQFHVMDLVRRdTQARNRVT-IVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03259 157 PLSALDAKLREELREELKE-LQRELGITtIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-234 |
3.15e-33 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 121.43 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLEsIIVVLR--- 103
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPsEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE-LVAIGRypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 -ASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRD 182
Cdd:PRK10575 114 hGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 183 TQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVY 234
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-219 |
1.01e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.09 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLN-NADGEALLDGEDLMSLSfaeraQKVVFLPQ--SLPQ 88
Cdd:cd03235 8 SYGGHPVLEDVSFEV-KPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPLEKER-----KRIGYVPQrrSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GVHLHVLESIIVVLRASGG---RDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:cd03235 82 DFPISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 166 ALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIALRHGDHVLMLkDGRLVASG 219
Cdd:cd03235 162 GVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
27-235 |
2.59e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.92 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQ---KVVFLPQSLPQGVHLHVLESIIV-- 100
Cdd:COG3638 26 IERGEFVALIGPSGAGKSTLLRCLNGLVEPTsGEILVDGQDVTALRGRALRRlrrRIGMIFQQFNLVPRLSVLTNVLAgr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 -----VLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHV 175
Cdd:COG3638 106 lgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 176 MDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETViTAERLAEVYR 235
Cdd:COG3638 186 MDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVLREIYG 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-215 |
8.58e-31 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 113.74 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 7 RSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE----RAQKVVF 81
Cdd:cd03255 8 KTYGGGGEKVQALKGVSLSI-EKGEFVAIVGPSGSGKSTLLNILGGLDRPTsGEVRVDGTDISKLSEKElaafRRRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQS---LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:cd03255 87 VFQSfnlLP---DLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 159 LLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIAlRHGDHVLMLKDGRL 215
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-214 |
1.99e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 112.56 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:cd03225 6 SFSYPDGARPALDDISLTI-KKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGKDLTKLSLKELRRKVGLVFQN- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 P--QGVHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd03225 84 PddQFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 165 SALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIALRHGDHVLMLKDGR 214
Cdd:cd03225 163 AGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-237 |
3.19e-30 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 113.01 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLESIivVLRASGGR 108
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL--ALHQPAGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP-------LSALDLNYQFHVMDLVRR 181
Cdd:COG4138 99 SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQlllldepMNSLDVAQQAALDRLLRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 182 DTQARNRVtIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVR 237
Cdd:COG4138 179 LCQQGITV-VMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
27-234 |
2.14e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaQKVVFLPQSLPQGVHLHVLESIIVVLRAS 105
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVLGEDVARDPAEVR-RRIGYVPQEPALYPDLTVRENLRFFARLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdtQA 185
Cdd:COG1131 102 G-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE--LA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 186 RNRVTIVVA-HDINIALRHGDHVLMLKDGRLVASGAPETvITAERLAEVY 234
Cdd:COG1131 179 AEGKTVLLStHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
27-232 |
3.42e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 109.73 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlP--QGVHLHVLESIIVVLR 103
Cdd:COG1122 24 IEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTsGEVLVDGKDITKKNLRELRRKVGLVFQN-PddQLFAPTVEEDVAFGPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpelllldepLSALDLNYQFHVMDLVRRdT 183
Cdd:COG1122 103 NLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEpevlvldepTAGLDPRGRRELLELLKR-L 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 184 QARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAE 232
Cdd:COG1122 181 NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLE 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-217 |
4.36e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.36 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 7 RSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERA----QKVVF 81
Cdd:COG1136 12 KSYGTGEGEVTALRGVSLSI-EAGEFVAIVGPSGSGKSTLLNILGGLDRPTsGEVLIDGQDISSLSERELArlrrRHIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQS---LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpell 158
Cdd:COG1136 91 VFQFfnlLP---ELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRpkli 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 159 lldeplSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIAlRHGDHVLMLKDGRLVA 217
Cdd:COG1136 167 ladeptGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
29-240 |
5.19e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVlESIIVVLRASG- 106
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDV-RQVVEMGRTPHr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 ---GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRR-- 181
Cdd:PRK09536 107 srfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRlv 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 182 DTqarNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRGRV 240
Cdd:PRK09536 187 DD---GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAV 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-226 |
1.35e-28 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 108.36 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAER---AQKVVF 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDV-RRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSEAELyrlRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSLPQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-235 |
2.36e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 108.15 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQ---KVVFLPQSLPQGVHLHVLESIIV---- 100
Cdd:TIGR02315 27 PGEFVAIIGPSGAGKSTLLRCINRLVEPSsGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNLIERLTVLENVLHgrlg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 ---VLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMD 177
Cdd:TIGR02315 107 ykpTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 178 LVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETvITAERLAEVYR 235
Cdd:TIGR02315 187 YLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRHIYG 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
27-229 |
7.43e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.15 E-value: 7.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLS---FAERAQKVVFLPQ----SL-PqgvHLHVLES 97
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGLLRPTsGSILFDGKDLTKLSrrsLRELRRRVQMVFQdpysSLnP---RMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 98 IIVVLRASGGRDNAQGRAQILAILEQLGithLALQYLD----QLSGGQRQLVGLAQSLIRRpelllldeplSALDLNYQF 173
Cdd:COG1123 365 IAEPLRLHGLLSRAERRERVAELLERVG---LPPDLADryphELSGGQRQRVAIARALALEpkllildeptSALDVSVQA 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 174 HVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITAER 229
Cdd:COG1123 442 QILNLL-RDLQRELGLTYLfISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-228 |
1.25e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSL-Pqgv 90
Cdd:COG3840 11 YGDFPLRFDLTIA---AGERVAILGPSGAGKSTLLNLIAGFLPPDsGRILWNGQDLTALPPAERPVSMLFQENNLfP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 HLHVLESIIVVLRaSGGRDNAQGRAQILAILEQLGITHLaLQYL-DQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDL 169
Cdd:COG3840 85 HLTVAQNIGLGLR-PGLKLTAEQRAQVEQALERVGLAGL-LDRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 170 NYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-225 |
1.61e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 102.55 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmslsfAERAQKVVFLPQS- 85
Cdd:cd03293 9 TYGGGGGAVTALEDISLSV-EEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPV-----TGPGPDRGYVFQQd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 --LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:cd03293 83 alLP---WLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 164 LSALD----LNYQFHVMDLVRrdtqaRNRVTIV-VAHDINIALRHGDHVLMLkdgrlvaSGAPETVI 225
Cdd:cd03293 159 FSALDaltrEQLQEELLDIWR-----ETGKTVLlVTHDIDEAVFLADRVVVL-------SARPGRIV 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-223 |
1.74e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.57 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKVVFl 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTI-KQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRSIQQRDICMVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 pQSLPQGVHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:PRK11432 85 -QSYALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 163 PLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPET 223
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-226 |
2.61e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 103.11 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE----RAQKVVFLPQS-- 85
Cdd:cd03294 33 KTGQTVGVNDVSLdVREGEIFVIMGLSGSGKSTLLRCINRLIEPTsGKVLIDGQDIAAMSRKElrelRRKKISMVFQSfa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 -LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd03294 113 lLP---HRTVLENVAFGLEVQG-VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 165 SALDlnyqfhvmDLVRRDTQ-------ARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:cd03294 189 SALD--------PLIRREMQdellrlqAELQKTIVfITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
3.13e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.79 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKV 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSI-EPGEFVALLGPSGCGKTTLLRMIAGFETPDsGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 80 VFlpQSL---PqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpe 156
Cdd:COG3842 82 VF--QDYalfP---HLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEpr 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 157 lllldepLSALDLNYQFHVMDLVRRdTQARNRVT-IVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:COG3842 156 vllldepLSALDAKLREEMREELRR-LQRELGITfIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-219 |
3.99e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 101.60 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-------GEALLDGEDLMSLSFAERaqKVVFLPQSLPQGVHLH 93
Cdd:cd03297 14 TLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlnGTVLFDSRKKINLPPQQR--KIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIIVVLRasgGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQF 173
Cdd:cd03297 92 VRENLAFGLK---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1167959503 174 HVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-217 |
4.16e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.19 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:COG1124 10 SYGQGGRRVPVLKDVSL-EVAPGESFGLVGESGSGKSTLLRALAGLERPWsGEVTFDGRPVTRRRRKAFRRRVQMVFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQGVhLH----VLESIIVVLRASGGRDNaqgRAQILAILEQLGIT-HLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:COG1124 88 PYAS-LHprhtVDRILAEPLRIHGLPDR---EERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVA 217
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-226 |
7.74e-26 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.22 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHV 94
Cdd:cd03295 14 KKAVNNLNLEI-AKGEFLVLIGPSGSGKTTTMKMINRLIEPTsGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 95 LESIIVVLRASG-GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQF 173
Cdd:cd03295 93 EENIALVPKLLKwPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 174 HVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-235 |
9.14e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.30 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 3 GLMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMS-LSFAERaqKVV 80
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEI-ASGELVALLGPSGSGKTTLLRIIAGLETPDsGRIVLNGRDLFTnLPPRER--RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 81 FLPQS---LPqgvHLHVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpel 157
Cdd:COG1118 79 FVFQHyalFP---HMTVAENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEpev 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 158 llldepLSALDlnyqFHVMDLVR---RDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEV 233
Cdd:COG1118 155 llldepFGALD----AKVRKELRrwlRRLHDELGGTTVfVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
..
gi 1167959503 234 YR 235
Cdd:COG1118 231 AR 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-217 |
1.00e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 101.32 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 7 RSFSAGYSTQPVIADLNvpL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSfAERAqkVVFlpQ 84
Cdd:COG1116 15 KRFPTGGGGVTALDDVS--LtVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTsGEVLVDGKPVTGPG-PDRG--VVF--Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 S---LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpelllld 161
Cdd:COG1116 88 EpalLP---WLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDpevllmd 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 162 epLSALD----LNYQFHVMDLVRrdtqaRNRVTIV-VAHDINIALRHGDHVLMLKD--GRLVA 217
Cdd:COG1116 164 epFGALDaltrERLQDELLRLWQ-----ETGKTVLfVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-219 |
1.38e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 97.58 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLN-NADGEALLDGEDLMSLS---FAERAQKVVFLP 83
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSI-KKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 Q----SL-PQgvhLHVLESIIVVLRASGGRDN-AQGRAQILAILEQLGithLALQYLD----QLSGGQRQLVGLAQSLIR 153
Cdd:cd03257 89 QdpmsSLnPR---MTIGEQIAEPLRIHGKLSKkEARKEAVLLLLVGVG---LPEEVLNryphELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-225 |
1.65e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.79 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaqKVVFLPQSLPQGVHLHVLESIIVVLRASGg 107
Cdd:cd03299 24 RGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNLPPEKR--DISYVPQNYALFPHMTVYKNIAYGLKKRK- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 108 RDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdTQARN 187
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK-IRKEF 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1167959503 188 RVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:cd03299 180 GVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-224 |
1.66e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 99.49 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 35 LLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFlpQSLPQGVHLHVLESIIVVLRASGgRDNAQG 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDsGSIMLDGEDVTNVPPHLRHINMVF--QSYALFPHMTVEENVAFGLKMRK-VPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 114 RAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQfHVMDLVRRDTQARNRVTIV- 192
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQLELKTIQEQLGITFVf 156
|
170 180 190
....*....|....*....|....*....|..
gi 1167959503 193 VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-154 |
2.55e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.02 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLESIIVVLRaS 105
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLL-L 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 106 GGRDNAQGRAQILAILEQLGITHLALQYLD----QLSGGQRQLVGLAQSLIRR 154
Cdd:pfam00005 87 KGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTK 139
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-236 |
3.71e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.93 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLESIivVLRASGGR 108
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYL--TLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY------QFHVMDLVRRD 182
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINPAGQLLLLDEPMnsldvaQQAALDRLLSE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 183 TQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRV 236
Cdd:PRK03695 179 LCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGV 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
27-234 |
4.61e-24 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 96.64 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSLPQgvHLHVLESIIVVLR-- 103
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDsGTILFGGEDATDVPVQERNVGFVFQHYALFR--HMTVFDNVAFGLRvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 -ASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRD 182
Cdd:cd03296 103 pRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 183 TQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVY 234
Cdd:cd03296 183 HDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-222 |
4.80e-24 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 96.54 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFlpQ 84
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDI-KEGEFFTLLGPSGCGKTTLLRLIAGFETPTsGEILLDGKDITNLPPHKRPVNTVF--Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 SLPQGVHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 165 SALDLNYQFHvMDLVRRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPE 222
Cdd:cd03300 159 GALDLKLRKD-MQLELKRLQKELGITFVfVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-219 |
6.25e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.78 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFl 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDI-ADGEFVVLLGPSGCGKTTTLRMIAGLEEPTsGRIYIGGRDVTDLPPKDRDIAMVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 pQSLPQGVHLHVLESIIVVLRaSGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:cd03301 79 -QNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 163 PLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-219 |
6.44e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 95.64 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSLpqGVH 91
Cdd:cd03298 10 YGEQPMHFDLTFA---QGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVTAAPPADRPVSMLFQENNL--FAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVlESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:cd03298 85 LTV-EQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1167959503 172 QFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-236 |
1.37e-23 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 95.31 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaQKVVFLPQSLPQGVH 91
Cdd:COG4555 11 YGKVPALKDVSF-TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDVRKEPREAR-RQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLRASGGRDnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:COG4555 89 LTVRENIRYFAELYGLFD-EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 172 QFHVMDLVRRDTqARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRV 236
Cdd:COG4555 168 RRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDA 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-232 |
1.70e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.06 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmSLSFAERA---QKV--VFlpQSL---PqgvH 91
Cdd:COG1126 21 SLDVE---KGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTITVDGEDL-TDSKKDINklrRKVgmVF--QQFnlfP---H 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSL-----------Irrpellll 160
Cdd:COG1126 92 LTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALamepkvmlfdeP-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 161 depLSALD-------LNyqfhVM-DLvrrdtqARNRVT-IVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA---E 228
Cdd:COG1126 164 ---TSALDpelvgevLD----VMrDL------AKEGMTmVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENpqhE 230
|
....
gi 1167959503 229 RLAE 232
Cdd:COG1126 231 RTRA 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-228 |
4.02e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 93.89 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNvpL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK----- 78
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVS--LdVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsGEILVDGQDITGLSEKELYELrrrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFlpQ------SLPqgvhlhVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLI 152
Cdd:COG1127 86 MLF--QggalfdSLT------VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 153 RRPELLLLDEPLSALD------LNyqfhvmDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:COG1127 158 LDPEILLYDEPTAGLDpitsavID------ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 1167959503 227 AE 228
Cdd:COG1127 232 SD 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
4.96e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.96 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFL 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSL-TLEAGECVAITGPSGSGKSTLLRALADLDPPTsGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 PQSlPQGVHLHVLESIIVVLRASGGRDNaqgRAQILAILEQLGITHLALQY-LDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:COG4619 80 PQE-PALWGGTVRDNLPFPFQLRERKFD---RERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRL 215
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-215 |
1.47e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 91.82 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLLpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLS--FAERAQKVVFLPQSLPQG 89
Cdd:cd03262 10 FGDFHVLKGIDLTVK-KGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKknINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 90 VHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDL 169
Cdd:cd03262 89 PHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1167959503 170 NYQFHVMDLVRRdtQARNRVT-IVVAHDINIALRHGDHVLMLKDGRL 215
Cdd:cd03262 169 ELVGEVLDVMKD--LAEEGMTmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-239 |
4.47e-22 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 92.20 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD---------GEALLDGEDLMSLSFAERAQKVVFLPQSLPQ 88
Cdd:PRK13547 16 ILRDLSLRIEP-GRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GVHLHVLEsiIVVL------RASGGRDNAQGRAqILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSL---------IR 153
Cdd:PRK13547 95 AFAFSARE--IVLLgryphaRRAGALTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEV 233
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARC 251
|
....*.
gi 1167959503 234 YRVRGR 239
Cdd:PRK13547 252 YGFAVR 257
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-224 |
5.06e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLpRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKVVFl 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIY-KGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDGVDLSHVPPYQRPINMMF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 pQSLPQGVHLHVLESIivvlrASGGRDNAQGRAQILA-ILEQLGITHL---ALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:PRK11607 98 -QSYALFPHMTVEQNI-----AFGLKQDKLPKAEIASrVNEMLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 159 LLDEPLSALDLN----YQFHVMDLVRRDTqarnrVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK11607 172 LLDEPMGALDKKlrdrMQLEVVDILERVG-----VTCVmVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-223 |
7.38e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 94.05 E-value: 7.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQS--LPQGvhl 92
Cdd:COG4988 350 RPALDGLSL-TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYsGSILINGVDLSDLDPASWRRQIAWVPQNpyLFAG--- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 hvleSIIVVLRasGGRDNAqGRAQILAILEQLGITHLaLQYLDQ------------LSGGQRQLVGLAQSLIRRPELLLL 160
Cdd:COG4988 426 ----TIRENLR--LGRPDA-SDEELEAALEAAGLDEF-VAALPDgldtplgeggrgLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 161 DEPLSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPET 223
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRR--LAKGRTVILITHRLA-LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-207 |
9.21e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 3 GLMLRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLN----NADGEALLDGEDLMSLSFAERaqK 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAP-GEILTLMGPSGSGKSTLLAAIAGTLspafSASGEVLLNGRRLTALPAEQR--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFLPQSLPQGVHLHVLESIIVVLRASGGRdnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 159 LLDEPLSALD--LNYQFHvmDLVRRDTQARNRVTIVVAHDINIALRHGDHV 207
Cdd:COG4136 156 LLDEPFSKLDaaLRAQFR--EFVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-214 |
1.27e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 88.07 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQ 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTL-KAGEIVALVGPNGSGKSTLLRAIAGLLKPTsGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 slpqgvhlhvlesiivvlrasggrdnaqgraqilaileqlgithlalqyldqLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 165 SALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIALRHGDHVLMLKDGR 214
Cdd:cd00267 109 SGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-224 |
2.62e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.29 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKV 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDL-DIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTsGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 80 VFlpQS---LPqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpe 156
Cdd:COG3839 80 VF--QSyalYP---HMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREpk 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 157 lllldepLSALDlnyqFHVMDLVR---RDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:COG3839 154 vflldepLSNLD----AKLRVEMRaeiKRLHRRLGTTTIyVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
35-242 |
3.53e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.99 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 35 LLGPNGCGKSTLLRSLAGLN--NADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQ--GVHLHVLESIIVVLRASGGR-- 108
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLppTYGNDVRLFGERRGGEDVWELRKRIGLVSPALQLrfPRDETVLDVVLSGFFDSIGLyr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 --DNAQgRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpelllldeplSALDLNYQFHVMDLVRRDTQAR 186
Cdd:COG1119 114 epTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDpellildeptAGLDLGARELLLALLDKLAAEG 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 187 NRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRGRVER 242
Cdd:COG1119 193 APTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEVER 248
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-224 |
5.69e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 90.17 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMS------LSFAERAQKVVFLPQSL-PqgvHLHVLESI 98
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDeGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLfP---HLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IVVLRASggrDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDL 178
Cdd:TIGR02142 97 RYGMKRA---RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1167959503 179 VRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-224 |
1.10e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.24 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN------ADGEALLDGEDLMSLSFA--ERAQ 77
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDI-PKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDGKDIYDLDVDvlELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVVFLPQSlPQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLD--QLSGGQRQLVGLAQSLIRRP 155
Cdd:cd03260 82 RVGMVFQK-PNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 156 ELLLLDEPLSALDLNYQFHVMDLVRRdtqARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAE---LKKEYTIViVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
27-219 |
1.10e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.95 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEdlmSLSFAERaQKVVFLPQSlpQGvhLHVLESIIVVLRAS 105
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILPDsGEVLFDGK---PLDIAAR-NRIGYLPEE--RG--LYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 G---GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRrd 182
Cdd:cd03269 95 AqlkGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIR-- 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1167959503 183 TQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03269 173 ELARAGKTVIlSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-215 |
1.39e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 86.84 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPllpRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQgvH 91
Cdd:TIGR01277 10 YEHLPMEFDLNVA---DGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFA--H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:TIGR01277 85 LTVRQNIGLGLHP-GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1167959503 172 QFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRL 215
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-229 |
2.22e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 86.72 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVV---F-LPQSLPqgvHLHVLESIIVV 101
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISGFLRPTsGSVLFDGEDITGLPPHEIARLGIgrtFqIPRLFP---ELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 LRASGG---------RDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLldeplsaLD---- 168
Cdd:cd03219 100 AQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLL-------LDepaa 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 169 -LNYQ--FHVMDLVRRdTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAER 229
Cdd:cd03219 173 gLNPEetEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-228 |
4.04e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.12 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:COG2274 480 SFRYPGDSPPVLDNISL-TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTsGRILIDGIDLRQIDPASLRRQIGVVLQD- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgVHLH---VLESIivvlraSGGRDNAqGRAQILAILEQLGIT----HLALQYL-------DQLSGGQRQLVGLAQSLI 152
Cdd:COG2274 558 ---VFLFsgtIRENI------TLGDPDA-TDEEIIEAARLAGLHdfieALPMGYDtvvgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 153 RRPELLLLDEPLSALDLNYQFHVMDLVRRDtqARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-220 |
4.26e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERA---QK--VVF-----LPq 84
Cdd:COG2884 15 REALSDVSLEI-EKGEFVFLTGPSGAGKSTLLKLLYGEERPTsGQVLVNGQDLSRLKRREIPylrRRigVVFqdfrlLP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 slpqgvHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLldepl 164
Cdd:COG2884 93 ------DRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL----- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 165 sA------LDLNYQFHVMDLVRRdtQARNRVTIVVA-HDINIALRHGDHVLMLKDGRLVASGA 220
Cdd:COG2884 161 -AdeptgnLDPETSWEIMELLEE--INRRGTTVLIAtHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-215 |
4.82e-20 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 84.37 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDlMSLSFAERAQKVVFLPQSLPQGVH 91
Cdd:cd03230 10 YGKKTALDDISLTV-EKGEIYGLLGPNGAGKTTLIKIILGLLKPDsGEIKVLGKD-IKKEPEEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLEsiivvlrasggrdnaqgraqilaileqlgithlalqYLDqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:cd03230 88 LTVRE------------------------------------NLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1167959503 172 QFHVMDLVRRdtQARNRVTIVVA-HDINIALRHGDHVLMLKDGRL 215
Cdd:cd03230 131 RREFWELLRE--LKKEGKTILLSsHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-225 |
5.15e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAE----RAQKVVFLPQSLPQGVHLHVLESIIVV 101
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 LRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRR 181
Cdd:PRK10070 131 MELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1167959503 182 DTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:PRK10070 210 LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-214 |
5.49e-20 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 83.97 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQS- 85
Cdd:cd03228 7 SFSYPGRPKPVLKDVSL-TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEILIDGVDLRDLDLESLRKNIAYVPQDp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 -LPQGvhlhvleSIivvlrasggRDNaqgraqilaileqlgIthlalqyldqLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:cd03228 86 fLFSG-------TI---------REN---------------I----------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 165 SALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGR 214
Cdd:cd03228 125 SALDPETEALILEALRA--LAKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-216 |
5.57e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 85.00 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQpVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLN-NADGEALLDGEDLmslSFAERAQKVVFLPQSL 86
Cdd:cd03226 6 SFSYKKGTE-ILDDLSLDL-YAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPI---KAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqGVHLH---VLESIIVvlrasGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:cd03226 81 --DYQLFtdsVREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 164 LSALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLV 216
Cdd:cd03226 154 TSGLDYKNMERVGELI-RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-221 |
1.18e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFlpQ 84
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTI-NNGEFLTLLGPSGCGKTTVLRLIAGFETPDsGRIMLDGQDITHVPAENRHVNTVF--Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 SLPQGVHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 165 SALDlnYQFHV-MDLVRRDTQARNRVT-IVVAHDINIALRHGDHVLMLKDGRLVASGAP 221
Cdd:PRK09452 173 SALD--YKLRKqMQNELKALQRKLGITfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-224 |
1.75e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 84.02 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQK-VVF 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTV-PEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSlpQGV--HLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGithlalQYLDQ----LSGGQRQLV---------- 145
Cdd:cd03224 80 VPEG--RRIfpELTVEENLLLGAYARRRAKRKARLERVYELFPRLK------ERRKQlagtLSGGEQQMLaiaralmsrp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 146 ----------GLAQSLIRRpelllldeplsaldlnyqfhVMDLVRRdtQARNRVTIV-VAHDINIALRHGDHVLMLKDGR 214
Cdd:cd03224 152 klllldepseGLAPKIVEE--------------------IFEAIRE--LRDEGVTILlVEQNARFALEIADRAYVLERGR 209
|
250
....*....|
gi 1167959503 215 LVASGAPETV 224
Cdd:cd03224 210 VVLEGTAAEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-257 |
2.07e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 85.92 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSlsfaerAQKVVFLP----------Q--SL 86
Cdd:COG4148 15 TLDVDFtLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsGRIRLGGEVLQD------SARGIFLPphrrrigyvfQeaRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQgvHLHVLESIIVVLRASGGrdnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:COG4148 89 FP--HLSVRGNLLYGRKRAPR---AERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 167 LDLNYQFHVMDLVRRdTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRGRVercsq 245
Cdd:COG4148 164 LDLARKAEILPYLER-LRDELDIPILyVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAG----- 237
|
250
....*....|..
gi 1167959503 246 gklqVVLDGVIA 257
Cdd:COG4148 238 ----SVLEATVA 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
27-234 |
2.50e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 84.32 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVV---F-LPQSLPqgvHLHVLESIIVV 101
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTLFNLITGFYRPTsGRILFDGRDITGLPPHRIARLGIartFqNPRLFP---ELTVLENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 LRASGG--------------RDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLirrpelllldeplsAL 167
Cdd:COG0411 104 AHARLGrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL--------------AT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 168 D------------LNYQ--FHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEV 233
Cdd:COG0411 170 EpklllldepaagLNPEetEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEA 249
|
.
gi 1167959503 234 Y 234
Cdd:COG0411 250 Y 250
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-214 |
2.96e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 82.23 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK---- 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNI-EAGEIVALLGPSGSGKSTLLRCIAGLEEPDsGSILIDGEDLTDLEDELPPLRrrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFLPQSLPQgvHLHVLESIivvlrasggrdnaqgraqilaileQLGithlalqyldqLSGGQRQLVGLAQSLIRRPELL 158
Cdd:cd03229 80 MVFQDFALFP--HLTVLENI------------------------ALG-----------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 159 LLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGR 214
Cdd:cd03229 123 LLDEPTSALDPITRREVRALL-KSLQAQLGITVVlVTHDLDEAARLADRVVVLRDGK 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
8.21e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALldgedlmslsfAERAQKVVFLPQ--SLPQ 88
Cdd:NF040873 1 GYGGRPVLHGVDLTI-PAGSLTAVVGPNGSGKSTLLKVLAGvLRPTSGTVR-----------RAGGARVAYVPQrsEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GVHLHVLESIIVVL---RASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:NF040873 69 SLPLTVRDLVAMGRwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1167959503 166 ALDLNYQFHVMDLVRRDTqARNRVTIVVAHDINIALRHgDHVLML 210
Cdd:NF040873 149 GLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-232 |
1.22e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK----VV 80
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNI-DQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVNDPKVDERLIRqeagMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 81 FlpQSLPQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLL 160
Cdd:PRK09493 83 F--QQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 161 DEPLSALDLNYQFHVMDlVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT---AERLAE 232
Cdd:PRK09493 161 DEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKnppSQRLQE 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-227 |
1.66e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 81.47 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 9 FSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RAQK----VVFl 82
Cdd:cd03258 11 FGDTGGKVTALKDVSLSV-PKGEIFGIIGRSGAGKSTLIRCINGLERPTsGSVLVDGTDLTLLSGKElRKARrrigMIF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 pqslpQGVHL----HVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:cd03258 89 -----QHFNLlssrTVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 159 LLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:cd03258 163 LCDEATSALDPETTQSILALL-RDINRELGLTIVlITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-222 |
3.35e-18 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.56 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPL---LPRGKITIL---------------LGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE 74
Cdd:COG4181 4 SSAPIIELRGLTKtvgTGAGELTILkgisleveagesvaiVGASGSGKSTLLGLLAGLDRPTsGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 75 RA----QKVVFLPQS---LPqgvHLHVLESIIVVLRASGGRDnAQGRAQilAILEQLGITHLALQYLDQLSGGQRQLVGL 147
Cdd:COG4181 84 RArlraRHVGFVFQSfqlLP---TLTALENVMLPLELAGRRD-ARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 148 AQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRhGDHVLMLKDGRLVASGAPE 222
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-227 |
3.67e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 82.02 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL----NNADGEALLDGEDLMSLSFAE----RAQKVVFLPQ----SL-PqgvHLH 93
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKElrkiRGREIQMIFQdpmtSLnP---VMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIIVVLRASGGRDNAQGRAQILAILEQLGITHlALQYLD----QLSGGQRQLVGLAQSLIrrpelllldepL----- 164
Cdd:COG0444 105 VGDQIAEPLRIHGGLSKAEARERAIELLERVGLPD-PERRLDryphELSGGMRQRVMIARALA-----------Lepkll 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 165 ------SALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:COG0444 173 iadeptTALDVTIQAQILNLL-KDLQRELGLAILfITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
13-228 |
4.55e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPllpRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQgvH 91
Cdd:PRK10771 11 YHHLPMRFDLTVE---RGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFS--H 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLrASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:PRK10771 86 LTVAQNIGLGL-NPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 172 QFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-230 |
5.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL----NNADGEALLDGEDLMSLSFAERAQKVVFLP 83
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSI-PRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLTAKTVWDIREKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 QSlP--QGVHLHVLESIivvlrASGGRDNAQGRAQILAI----LEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPEL 157
Cdd:PRK13640 91 QN-PdnQFVGATVGDDV-----AFGLENRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 158 LLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIAlRHGDHVLMLKDGRLVASGAPETVITAERL 230
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLI-RKLKKKNNLTVIsITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-240 |
1.23e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.90 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERaqKVVFLPQSLPQGVHLHVLESI---IVVL 102
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVSRLHARDR--KVGFVFQHYALFRHMTVFDNIafgLTVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 103 RASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRD 182
Cdd:PRK10851 103 PRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 183 TQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV-------ITAERLAEVYRVRGRV 240
Cdd:PRK10851 183 HEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrFVLEFMGEVNRLQGTI 247
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-234 |
1.31e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.12 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLLpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK-VVFLPQ--SLPQ 88
Cdd:cd03218 10 YGKRKVVNGVSLSVK-QGEIVGLLGPNGAGKTTTFYMIVGLVKPDsGKILLDGQDITKLPMHKRARLgIGYLPQeaSIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GvhLHVLESIIVVLRaSGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALD 168
Cdd:cd03218 89 K--LTVEENILAVLE-IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 169 ----LNYQFHVMDLVRR-------DTQARNRVTIVvahdinialrhgDHVLMLKDGRLVASGAPETVITAERLAEVY 234
Cdd:cd03218 166 piavQDIQKIIKILKDRgigvlitDHNVRETLSIT------------DRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
27-219 |
2.90e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 77.62 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGkITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaQKVVFLPQSLPQGVHLHVLESIIVVLRAS 105
Cdd:cd03264 23 LGPG-MYGLLGPNGAGKTTLMRILATLTPPSsGTIRIDGQDVLKQPQKLR-RRIGYLPQEFGVYPNFTVREFLDYIAWLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGRDnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdtQA 185
Cdd:cd03264 101 GIPS-KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE--LG 177
|
170 180 190
....*....|....*....|....*....|....
gi 1167959503 186 RNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03264 178 EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-245 |
3.87e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNAD----------GEALLDGEDLMSLSFAERAQkVVFLPQSLPQGV 90
Cdd:PRK09984 24 DLNIH---HGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQREGRLARDIRKSRAN-TGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 HLHVLESIIV-------VLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:PRK09984 100 RLSVLENVLIgalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 164 LSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETvITAERLAEVYRVRGRVERC 243
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDNERFDHLYRSINRVEEN 258
|
..
gi 1167959503 244 SQ 245
Cdd:PRK09984 259 AK 260
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-219 |
6.19e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.86 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAII-GRVGSGKSTLLKLLAGLYKPtSGSVLLDGTDIRQLDPADLRRNIGYVPQD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgvhlhvlesiiVVLRASGGRDN-AQGR-----AQILAILEQLGITHLALQY---LD--------QLSGGQRQLVGLAQ 149
Cdd:cd03245 87 -------------VTLFYGTLRDNiTLGApladdERILRAAELAGVTDFVNKHpngLDlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 150 SLIRRPELLLLDEPLSALDLNYQFHVMDlvRRDTQARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASG 219
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKE--RLRQLLGDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-168 |
6.66e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.59 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGY----STQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSfAER 75
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSL-TIESGEFVVALGASGCGKTTLLNLIAGfLAPSSGEITLDGVPVTGPG-ADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 76 AqkVVFLPQSL-PQgvhLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRR 154
Cdd:COG4525 79 G--VVFQKDALlPW---LNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 1167959503 155 PELLLLDEPLSALD 168
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-234 |
1.03e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.56 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVI--ADLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQK-VVF 81
Cdd:COG0410 6 VENLHAGYGGIHVLhgVSLEVE---EGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSlpQGV--HLHVLESIIVVLRASGGRDNAQGR-AQILAILEQLGithlalQYLDQ----LSGGQRQLV--------- 145
Cdd:COG0410 83 VPEG--RRIfpSLTVEENLLLGAYARRDRAEVRADlERVYELFPRLK------ERRRQragtLSGGEQQMLaigralmsr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 146 -----------GLAQSLIRRpelllldeplsaldlnyqfhVMDLVRRdtQARNRVTIVVA-HDINIALRHGDHVLMLKDG 213
Cdd:COG0410 155 pklllldepslGLAPLIVEE--------------------IFEIIRR--LNREGVTILLVeQNARFALEIADRAYVLERG 212
|
250 260
....*....|....*....|.
gi 1167959503 214 RLVASGAPETVITAERLAEVY 234
Cdd:COG0410 213 RIVLEGTAAELLADPEVREAY 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-225 |
1.13e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 79.04 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:COG4987 340 SFRYPGAGRPVLDGLSL-TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGGVDLRDLDEDDLRRRIAVVPQR- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgVHLH---VLESIIVvlrasgGRDNAqGRAQILAILEQLGITHLALQY---LD--------QLSGGQRQLVGLAQSLI 152
Cdd:COG4987 418 ---PHLFdttLRENLRL------ARPDA-TDEELWAALERVGLGDWLAALpdgLDtwlgeggrRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 153 RRPELLLLDEPLSALDLNYQFHVMDLVRrdTQARNRVTIVVAHDInIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLL--EALAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-227 |
1.52e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.57 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAE-----RAQKVVFlpQ----SL-PQgvhLHVLE 96
Cdd:COG4172 309 LRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVF--QdpfgSLsPR---MTVGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 97 SIIVVLRASG-GRDNAQGRAQILAILEQLGITHLALQ-YLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFH 174
Cdd:COG4172 384 IIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 175 VMDLVrRDTQARNRVT-IVVAHDINI--ALRHgdHVLMLKDGRLVASGAPETVITA 227
Cdd:COG4172 464 ILDLL-RDLQREHGLAyLFISHDLAVvrALAH--RVMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-214 |
4.19e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 74.44 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmSLSFAERAQKVVFL 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAA-GEALALTGPNGSGKTTLLRILAGLLPPSaGEVLWNGEPI-RDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 PQSLPQGVHLHVLESIIVVLRASGGRDNaqgRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD---REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 163 PLSALDLNYQFHVMDLVRRdtQARNRVTIVVA--HDINIAlrhGDHVLMLKDGR 214
Cdd:COG4133 158 PFTALDAAGVALLAELIAA--HLARGGAVLLTthQPLELA---AARVLDLGDFK 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-235 |
4.52e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA------DGEALLDGEDLMS----LSFAERAQ 77
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGF-PARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrySGDVLLGGRSIFNyrdvLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVVFLPQSLPqgvhLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLD----QLSGGQRQLVGLAQSLIR 153
Cdd:PRK14271 105 MLFQRPNPFP----MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVRrdTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEV 233
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIR--SLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
..
gi 1167959503 234 YR 235
Cdd:PRK14271 259 AR 260
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-238 |
5.06e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 74.50 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEdlmslSFAERAQKVVFLPQ------SLPQGVHLHVLES---I 98
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLiPPAKGTVKVAGA-----SPGKGWRHIGYVPQrhefawDFPISVAHTVMSGrtgH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IVVLRASGGRDNAQGRAQilaiLEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDL 178
Cdd:TIGR03771 80 IGWLRRPCVADFAAVRDA----LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 179 VRRDTQARNRVtIVVAHDINIALRHGDHVLMLkDGRLVASGAPETVITAERLAEVYRVRG 238
Cdd:TIGR03771 156 FIELAGAGTAI-LMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGVSD 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
7.87e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.71 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEdlMSLSFAERAQKVVFlp 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDL-HIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT--APLAEAREDTRLMF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 qslpQGVHLHVLESII--VVLRASGgrdnaQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:PRK11247 88 ----QDARLLPWKKVIdnVGLGLKG-----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRL 215
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-221 |
8.65e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 73.69 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaQKVVFLPQSLPQGV 90
Cdd:cd03263 11 KKGTKPAVDDLSLNV-YKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYINGYSIRTDRKAAR-QSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 HLHVLESIIVVLRASGGRdNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLN 170
Cdd:cd03263 89 ELTVREHLRFYARLKGLP-KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 171 YQFHVMDLVRRdtQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAP 221
Cdd:cd03263 168 SRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-225 |
1.29e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 73.41 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQS--LPQGVhlh 93
Cdd:cd03254 17 PVLKDINF-SIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDtfLFSGT--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIIVvlrasgGRDNAQgRAQILAILEQLGITHLALQ----YLDQ-------LSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:cd03254 93 IMENIRL------GRPNAT-DEEVIEAAKEAGAHDFIMKlpngYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 163 PLSALDLNYQFHVMDLVRRDTQarNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLST-IKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-215 |
1.89e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.83 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLsfaeRAQKVVFLPQSLpqGV----- 90
Cdd:cd03292 15 AALDGINISI-SAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDL----RGRAIPYLRRKI--GVvfqdf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 ----HLHVLESIIVVLRASG-GRDNAQGRaqILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:cd03292 88 rllpDRNVYENVAFALEVTGvPPREIRKR--VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 166 ALDLNYQFHVMDLVRRDTQArnRVTIVVA-HDINIALRHGDHVLMLKDGRL 215
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKA--GTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-232 |
4.67e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLLPRGkITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEdlmSLSFAERA-----QKVVFLPQSL 86
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSP-VTGLVGANGCGKSTLFMNLSGLlRPQKGAVLWQGK---PLDYSKRGllalrQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 167 LDLNYQFHVMDLVRRDTQARNRVtIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAE 232
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-219 |
5.51e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEdlmSLSFAERA---------QKV--V 80
Cdd:COG4161 12 YGSHQALFDINLEC-PSGETLVLLGPSGAGKSSLLRVLNLLETPDsGQLNIAGH---QFDFSQKPsekairllrQKVgmV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 81 FLPQSL-PqgvHLHVLESIIV----VLRASggRDNAQGRAQilAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRP 155
Cdd:COG4161 88 FQQYNLwP---HLTVMENLIEapckVLGLS--KEQAREKAM--KLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 156 ELLLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-224 |
7.42e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDlmsLSFAERaQKVVFLP------QSLPqgvhlhVLESII- 99
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPDsGEVLWDGEP---LDPEDR-RRIGYLPeerglyPKMK------VGEQLVy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 100 -VVLRasgGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpelllldeplSALD-LNYQfHVMD 177
Cdd:COG4152 95 lARLK---GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDpellildepfSGLDpVNVE-LLKD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1167959503 178 LVRRdtQARNRVTIVVA-HDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:COG4152 171 VIRE--LAAKGTTVIFSsHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-227 |
7.88e-15 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 73.75 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgvhl 92
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAII-GRIGSGKSTLLKLLLGLYQPTeGSVLLDGVDIRQIDPADLRRNIGYVPQD------- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 hvlesiiVVLRASGGRDN-AQGRAQ-----ILAILEQLGITHLALQY---LD--------QLSGGQRQLVGLAQSLIRRP 155
Cdd:TIGR03375 548 -------PRLFYGTLRDNiALGAPYaddeeILRAAELAGVTEFVRRHpdgLDmqigergrSLSGGQRQAVALARALLRDP 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 156 ELLLLDEPLSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:TIGR03375 621 PILLLDEPTSAMDNRSEERFKDRLKR--WLAGKTLVLVTHRTSL-LDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-219 |
1.83e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKVvflpQSLPQGV-- 90
Cdd:PRK11124 12 YGAHQALFDITLDC-PQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAI----RELRRNVgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 ---------HLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:PRK11124 87 vfqqynlwpHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 162 EPLSALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:PRK11124 167 EPTAALDPEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-221 |
2.76e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKV 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDI-HEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 80 VFlpQSLPQGVHLHVLESIIVVLRASG-GRDNAQGRAQILAILEQLGitHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:PRK11000 80 VF--QSYALYPHLSVAENMSFGLKLAGaKKEEINQRVNQVAEVLQLA--HLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 159 LLDEPLSALD--LNYQFHVMdlVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAP 221
Cdd:PRK11000 156 LLDEPLSNLDaaLRVQMRIE--ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-222 |
4.27e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL-NNADGE-ALLDGEDLMslsfaeraqkvvFLPQS--LPQGVh 91
Cdd:COG4178 376 RPLLEDLSLSL-KPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRiARPAGARVL------------FLPQRpyLPLGT- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 lhvlesiivvLRAS---GGRDNAQGRAQILAILEQLGITHLALQyLDQ-------LSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:COG4178 442 ----------LREAllyPATAEAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 162 EPLSALDLNYQFHVMDLVRrdtQARNRVTIV-VAHDINIALRHgDHVLMLK---DGRLVASGAPE 222
Cdd:COG4178 511 EATSALDEENEAALYQLLR---EELPGTTVIsVGHRSTLAAFH-DRVLELTgdgSWQLLPAEAPA 571
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-219 |
5.42e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSagYSTQP---VIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLP 83
Cdd:TIGR00958 485 SFS--YPNRPdvpVLKGLTFTLHP-GEVVALVGPSGSGKSTVAALLQNLYQPTgGQVLLDGVPLVQYDHHYLHRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 Q-----------SLPQGVHLHVLESIIVVLRASGGRDNAQGRAQilaileqlGITHLALQYLDQLSGGQRQLVGLAQSLI 152
Cdd:TIGR00958 562 QepvlfsgsvreNIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN--------GYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 153 RRPELLLLDEPLSALDLNYQFhvmdLVRRDTQARNRVTIVVAHDINIAlRHGDHVLMLKDGRLVASG 219
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-234 |
5.58e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKV 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTV-NSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 80 V-FLPQSLPQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELL 158
Cdd:PRK10895 80 IgYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 159 LLDEPLSALDlnyQFHVMDLVRRDTQARNR--VTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVY 234
Cdd:PRK10895 160 LLDEPFAGVD---PISVIDIKRIIEHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-224 |
7.62e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLmslsfaeraqKVVFLPQS 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKP-GKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL----------RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 LPQGVHLHVLESIIVVLRAsggrdnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRP------GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 166 ALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLkDGRLVASGAPETV 224
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVV 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-215 |
7.95e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 67.63 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEP-GESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGADISQWDPNELGDHVGYLPQD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgvhlhvlesiiVVLRASGGRDNAqgraqilaileqlgithlalqyldqLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:cd03246 85 -------------DELFSGSIAENI-------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 167 LDLNYQFHVMDLVRRdTQARNRVTIVVAHDINiALRHGDHVLMLKDGRL 215
Cdd:cd03246 127 LDVEGERALNQAIAA-LKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
28-200 |
8.22e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 67.83 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGE--DLMSLSFAERAQKVVFLPQSlP--QGVHLHVLESIIVVL 102
Cdd:TIGR01166 16 ERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQD-PddQLFAADVDQDVAFGP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 103 RASGGRDnAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRD 182
Cdd:TIGR01166 95 LNLGLSE-AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRL 173
|
170
....*....|....*...
gi 1167959503 183 TQARNRVtIVVAHDINIA 200
Cdd:TIGR01166 174 RAEGMTV-VISTHDVDLA 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-240 |
8.74e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLN-------NADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQ 88
Cdd:PRK14246 23 KAILKDITIKI-PNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 165 SALDLnyqFHVMDLVRRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITAER--LAEVYrVRGRV 240
Cdd:PRK14246 182 SMIDI---VNSQAIEKLITELKNEIAIViVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKneLTEKY-VIGRI 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-230 |
1.20e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 68.68 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQ-----KVVFlpQSLPQG 89
Cdd:TIGR02769 24 APVLTNVSLSI-EEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVF--QDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 90 VH--LHVLESIIVVLRASGGRDNAQGRAQILAILEQLGI-THLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:TIGR02769 101 VNprMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 167 LDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVasgapETVITAERL 230
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV-----EECDVAQLL 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-215 |
1.86e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 67.50 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSagYSTQP---VIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKVVFLP 83
Cdd:cd03248 18 TFA--YPTRPdtlVLQDVSFTLHP-GEVTALVGPSGSGKSTVVALLENFYQpQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 Q-----------SLPQGVHLHVLESIIVVLRASGGRDNAQGRAQilaileqlGITHLALQYLDQLSGGQRQLVGLAQSLI 152
Cdd:cd03248 95 QepvlfarslqdNIAYGLQSCSFECVKEAAQKAHAHSFISELAS--------GYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 153 RRPELLLLDEPLSALDLNYQFHVMDLVRRDTQarNRVTIVVAHDINIaLRHGDHVLMLKDGRL 215
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
28-219 |
2.50e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 67.01 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaQKVVFLPQSLPQGVHLHVLESIIVVLRASG 106
Cdd:cd03266 29 KPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKEPAEAR-RRLGFVSDSTGLYDRLTARENLEYFAGLYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 -GRDNAQGRAQILAilEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdTQA 185
Cdd:cd03266 108 lKGDELTARLEELA--DRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRA 184
|
170 180 190
....*....|....*....|....*....|....
gi 1167959503 186 RNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03266 185 LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-210 |
3.28e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRS--FSAGysTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVV 80
Cdd:PRK10247 8 LQLQNvgYLAG--DAKILNNISFSLRA-GEFKLITGPSGCGKSTLLKIVASLISPTsGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 81 FLPQSlPQGVHLHVLESIIVVLRAsggRDNAQGRAQILAILEQLGITHLALQY-LDQLSGGQRQLVGLAQSLIRRPELLL 159
Cdd:PRK10247 85 YCAQT-PTLFGDTVYDNLIFPWQI---RNQQPDPAIFLDDLERFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 160 LDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINiALRHGDHVLML 210
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-201 |
3.83e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSfAERAqkVVFL 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLES-GELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPG-AERG--VVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 83 PQSL-PQgvhLHVLESIIVVLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:PRK11248 78 NEGLlPW---RNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIAL 201
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-215 |
3.99e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLS----FAERAQKVVFLPQSLPQGVHLHVLESIIVVLR 103
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGsSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNaQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDT 183
Cdd:PRK10584 115 LRGESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
|
170 180 190
....*....|....*....|....*....|..
gi 1167959503 184 QARNRVTIVVAHDINIALRhGDHVLMLKDGRL 215
Cdd:PRK10584 194 REHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-232 |
4.01e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RAQKVVFLPQSL---PqgvHLHVLESI-IV 100
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGVYQPDsGEILLDGEPVRFRSPRDaQAAGIAIIHQELnlvP---NLSVAENIfLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 VLRASGGR-DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQslirrpelllldeplsALDLNYQFHVMD-- 177
Cdd:COG1129 104 REPRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR----------------ALSRDARVLILDep 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 178 ---LVRRDTQA--------RNR-VTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETViTAERLAE 232
Cdd:COG1129 168 tasLTEREVERlfriirrlKAQgVAIIyISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL-TEDELVR 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-236 |
4.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEI-NEGEYVAILGHNGSGKSTISKILTGLLKPqSGEIKIDGITISKENLKEIRKKIGIIFQN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 P--QGVHLHVLESIivvlrASGGRDNAQGRAQILAIleqlgITHLALQ-----YLDQ----LSGGQRQLVGLAQSLIRRP 155
Cdd:PRK13632 92 PdnQFIGATVEDDI-----AFGLENKKVPPKKMKDI-----IDDLAKKvgmedYLDKepqnLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 156 ELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRhGDHVLMLKDGRLVASGAPETVITAERLAEVYR 235
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEKAK 240
|
.
gi 1167959503 236 V 236
Cdd:PRK13632 241 I 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-253 |
4.24e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGedlMSLSFAERAQKVVFLPQSLPQGVHLHVLESIIVVLRAS 105
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGfVRLASGKISILG---QPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GG-----RDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVr 180
Cdd:PRK15056 107 GHmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL- 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 181 RDTQARNRVTIVVAHDINIALRHGDHVLMLKdGRLVASGAPETVITAERLAEVYRVRGRVERCSQGKLQVVLD 253
Cdd:PRK15056 186 RELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFSGVLRHVALNGSEESIITD 257
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-240 |
4.67e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVPLLPRgKITILLGPNGCGKSTLLRSLAGL------NNADGEALLDGEDLMSLSFAE 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDN-TITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 75 ---RAQKVVFLPQSLPqgvHLHVLESIIVVLRASG-GRDNAQGRAQILAILEQLGITHLALQYLD----QLSGGQRQLVG 146
Cdd:PRK14247 80 lrrRVQMVFQIPNPIP---NLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 147 LAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrrdTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLF---LELKKDMTIVlVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|....*..
gi 1167959503 226 TAER--LAEVYrVRGRV 240
Cdd:PRK14247 234 TNPRheLTEKY-VTGRL 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-222 |
5.02e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNN---ADGEALLDGEDLMSLSFAERAQKVVFL----PQSLPqGVhlh 93
Cdd:COG0396 20 NLTIK---PGEVHAIMGPNGSGKSTLAKVLMGHPKyevTSGSILLDGEDILELSPDERARAGIFLafqyPVEIP-GV--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 vleSIIVVLRASGGR------DNAQGRAQILAILEQLGITHLALQ-YLDQ-LSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:COG0396 93 ---SVSNFLRTALNArrgeelSAREFLKLLKEKMKELGLDEDFLDrYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 166 ALDLnyqfhvmDLVR------RDTQARNRVTIVVAHDINIaLRHG--DHVLMLKDGRLVASGAPE 222
Cdd:COG0396 170 GLDI-------DALRivaegvNKLRSPDRGILIITHYQRI-LDYIkpDFVHVLVDGRIVKSGGKE 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
29-159 |
5.39e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK-VVFLPQ--SLPQGvhLHVLESIIVVLRA 104
Cdd:COG1137 28 QGEIVGLLGPNGAGKTTTFYMIVGLVKPDsGRIFLDGEDITHLPMHKRARLgIGYLPQeaSIFRK--LTVEDNILAVLEL 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 105 SGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLL 159
Cdd:COG1137 106 RK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-219 |
6.60e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 67.82 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQslpqgvHLHVL 95
Cdd:TIGR02203 346 PALDSISL-VIEPGETVALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQ------DVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVVLRASGGRDNAqGRAQILAILEQLGITHLALQY---LDQ--------LSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:TIGR02203 419 NDTIANNIAYGRTEQA-DRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 165 SALDLNYQFHVMDLVRRDTQarNRVTIVVAHDINiALRHGDHVLMLKDGRLVASG 219
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-231 |
8.15e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-----RAQKVVFlpQSLPQGVHLH--VLESI 98
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSqGNVSWRGEPLAKLNRAQrkafrRDIQMVF--QDSISAVNPRktVREII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IVVLRASGGRDNAQGRAQILAILEQLGITHLALQYL-DQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMD 177
Cdd:PRK10419 113 REPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 178 LVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVasgapETVITAERLA 231
Cdd:PRK10419 193 LLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV-----ETQPVGDKLT 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-213 |
9.83e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.56 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSfAERAqkVVFLPQSL-PQgvhLHVLESI-IVVLRAS 105
Cdd:TIGR01184 10 QGEFISLIGHSGCGKSTLLNLISGLAQpTSGGVILEGKQITEPG-PDRM--VVFQNYSLlPW---LTVRENIaLAVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDL----NYQFHVMDLVRr 181
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQEELMQIWE- 162
|
170 180 190
....*....|....*....|....*....|...
gi 1167959503 182 dtqaRNRVT-IVVAHDINIALRHGDHVLMLKDG 213
Cdd:TIGR01184 163 ----EHRVTvLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-227 |
1.16e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.02 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKS----TLLRSLA-GLNNADGEALLDGEDLMSLSFAE----RAQK 78
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDI-AAGETLALVGESGSGKSvtalSILRLLPdPAAHPSGSILFDGQDLLGLSERElrriRGNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFLPQ----SL-PqgvhLHVLESIIV-VLRASGGRDNAQGRAQILAILEQLGITHLAL---QYLDQLSGGQRQLVGLAQ 149
Cdd:COG4172 94 IAMIFQepmtSLnP----LHTIGKQIAeVLRLHRGLSGAAARARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 150 SLIRRPELLLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLL-KDLQRELGMALLlITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-219 |
1.27e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 64.26 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSfAERAQKVVFLPQSl 86
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALL-GRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISVLNQR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgVHLHVLesiivvlrasggrdnaqgraqilAILEQLGIthlalqyldQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:cd03247 84 ---PYLFDT-----------------------TLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 167 LDLNYQFHVMDLVRRdtQARNRVTIVVAHDInIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03247 129 LDPITERQLLSLIFE--VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-210 |
1.64e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 66.54 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 15 TQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSlPQGVHLH 93
Cdd:TIGR02857 334 RRPALRPVSF-TVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVNGVPLADADADSWRDQIAWVPQH-PFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIivVLRASGGRDNAQGRAQILAILEQL------GITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSAL 167
Cdd:TIGR02857 412 IAENI--RLARPDASDAEIREALERAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1167959503 168 DLNYQFHVMDLVRRdtQARNRVTIVVAHDINIALRhGDHVLML 210
Cdd:TIGR02857 490 DAETEAEVLEALRA--LAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-219 |
1.99e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 64.60 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL----NNADGEALLDGE----DLMSLSFAERAQKVVFLPqslpqg 89
Cdd:cd03234 22 ILNDVSLHV-ESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFNGQprkpDQFQKCVAYVRQDDILLP------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 90 vHLHVLESIIVVLRASGGRDNAQGRAQILA---ILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:cd03234 95 -GLTVRETLTYTAILRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 167 LDLNYQFHVMDLVRRdTQARNRVTIVVAH----DIniaLRHGDHVLMLKDGRLVASG 219
Cdd:cd03234 174 LDSFTALNLVSTLSQ-LARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-222 |
3.55e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.79 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLmlrSFSAGysTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLS---FAERA 76
Cdd:PRK11831 10 MRGV---SFTRG--NRCIFDNISLTV-PRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEILFDGENIPAMSrsrLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 77 QKVVFLPQSLPQGVHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPE 156
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 157 LLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPE 222
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
35-232 |
4.53e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 64.05 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 35 LLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLM-------SLSFAERAQ--------KVVFlpQSLPQGVHLHVLESI 98
Cdd:COG4598 39 IIGSSGSGKSTFLRCINLLETPDsGEIRVGGEEIRlkpdrdgELVPADRRQlqrirtrlGMVF--QSFNLWSHMTVLENV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IV----VLrasgGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFH 174
Cdd:COG4598 117 IEapvhVL----GRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 175 VMdLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA---ERLAE 232
Cdd:COG4598 193 VL-KVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNpksERLRQ 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-233 |
4.71e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 64.71 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIA----DLNVPllpRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RAQK----VVFlpqs 85
Cdd:COG1135 16 GPVTAlddvSLTIE---KGEIFGIIGYSGAGKSTLIRCINLLERPTsGSVLVDGVDLTALSERElRAARrkigMIF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 lpQGVHL----HVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRpelllld 161
Cdd:COG1135 89 --QHFNLlssrTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNpkvllcd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 162 eplSALDLNYQFHVMDLVrRDTQARNRVTIVVA-HDINIALRHGDHVLMLKDGRLVASG-------APETVITAERLAEV 233
Cdd:COG1135 166 eatSALDPETTRSILDLL-KDINRELGLTIVLItHEMDVVRRICDRVAVLENGRIVEQGpvldvfaNPQSELTRRFLPTV 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-215 |
6.83e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERA----QKVVFLPQS---LPQgvhLHVLESIIV 100
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFhhlLPD---FTALENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 VLRAsGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVR 180
Cdd:PRK11629 111 PLLI-GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLG 189
|
170 180 190
....*....|....*....|....*....|....*
gi 1167959503 181 RDTQARNRVTIVVAHDINIALRHGDHVLMlKDGRL 215
Cdd:PRK11629 190 ELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-227 |
7.35e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQK---------VVFLPQSLPQGVHLHVLESII- 99
Cdd:PRK11264 29 GEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKglirqlrqhVGFVFQNFNLFPHRTVLENIIe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 100 --VVLRASGgRDNAQGRAQilAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMD 177
Cdd:PRK11264 109 gpVIVKGEP-KEEATARAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 178 LVRRDTQARnRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:PRK11264 186 TIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
9.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVpLLPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGE--DLMSLSFAERAQKVVFLPQSlPQgvhlHVLES 97
Cdd:PRK13636 24 GINI-NIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQD-PD----NQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 98 IIVVLRASGGRDNAQ-----GRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQ 172
Cdd:PRK13636 98 ASVYQDVSFGAVNLKlpedeVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 173 FHVMDLVrRDTQARNRVTIVVA-HDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK13636 178 SEIMKLL-VEMQKELGLTIIIAtHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-238 |
1.12e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNADGEAL-LDGEDLMSLSFAERaQKVVFLPQSLPQGVH 91
Cdd:PRK13537 17 YGDKLVVDGLSFHVQR-GECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHAR-QRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:PRK13537 95 FTVRENLLVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 172 QfHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVYRVRG 238
Cdd:PRK13537 174 R-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIYG 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-233 |
1.25e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RA--QKVVFLPQslpqgvH 91
Cdd:PRK11153 17 TIHALNNVSLhIPAGEIFGVIGASGAGKSTLIRCINLLERPTsGRVLVDGQDLTALSEKElRKarRQIGMIFQ------H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVV------LRASgGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:PRK11153 91 FNLLSSRTVFdnvalpLELA-GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 166 ALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGA-------PETVITAERLAEV 233
Cdd:PRK11153 170 ALDPATTRSILELL-KDINRELGLTIVlITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHPLTREFIQST 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-216 |
1.62e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.41 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 32 ITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKV--VFlpQSLPQGV--HLHVLESIIVVLRASG 106
Cdd:COG1101 35 VTVI-GSNGAGKSTLLNAIAGSLPPDsGSILIDGKDVTKLPEYKRAKYIgrVF--QDPMMGTapSMTIEENLALAYRRGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 GRD-----NAQGRAQILAILEQLGithLALQ-YLDQ----LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVM 176
Cdd:COG1101 112 RRGlrrglTKKRRELFRELLATLG---LGLEnRLDTkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1167959503 177 DLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLV 216
Cdd:COG1101 189 ELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
16-232 |
1.64e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 62.28 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNN---ADGEALLDGEDLMSLSFAERAQKVVFL----PQSLPQ 88
Cdd:TIGR01978 13 KEILKGVNLTV-KKGEIHAIMGPNGSGKSTLSKTIAGHPSyevTSGTILFKGQDLLELEPDERARAGLFLafqyPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 GVHLHVLESIIVVLRASGGR---DNAQGRAQILAILEQLGIT-HLALQYLDQ-LSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:TIGR01978 92 VSNLEFLRSALNARRSARGEeplDLLDFEKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 164 LSALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIA-LRHGDHVLMLKDGRLVASGAPEtviTAERLAE 232
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINR-LREPDRSFLIITHYQRLLnYIKPDYVHVLLDGRIVKSGDVE---LAKELEA 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-228 |
1.73e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RAQKVVflpqs 85
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALL-GRTGCGKSTLLQLLTRAWDPQqGEILLNGQPIADYSEAAlRQAISV----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 LPQGVHL--HVLesiivvlrasggRDN---AQGRA---QILAILEQLGITHLA--LQYLD--------QLSGGQRQLVGL 147
Cdd:PRK11160 419 VSQRVHLfsATL------------RDNlllAAPNAsdeALIEVLQQVGLEKLLedDKGLNawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 148 AQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRrdTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
.
gi 1167959503 228 E 228
Cdd:PRK11160 564 Q 564
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-221 |
2.29e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.49 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPLLpRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERaQKVVFLPQSLPQGVHL 92
Cdd:TIGR01257 941 SGRPAVDRLNITFY-ENQITAFLGHNGAGKTTTLSILTGLlPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 HVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQ 172
Cdd:TIGR01257 1019 TVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 173 FHVMDLVRRdtQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAP 221
Cdd:TIGR01257 1098 RSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
28-222 |
2.31e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 61.62 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAqKVVFLPQSLPQGVHLHVLESIIVVLRASG 106
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHDVVREPREVRR-RIGIVFQDLSVDDELTGWENLYIHARLYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 GRdNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrRDTQAR 186
Cdd:cd03265 103 VP-GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI-EKLKEE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1167959503 187 NRVTIVV-AHDINIALRHGDHVLMLKDGRLVASGAPE 222
Cdd:cd03265 181 FGMTILLtTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-222 |
2.33e-11 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 61.86 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYST-QPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDL--MSLSFAERAQKVVflpqslP 87
Cdd:cd03253 9 AYDPgRPVLKDVSFTIPA-GKKVAIVGPSGSGKSTILRLLFRFyDVSSGSILIDGQDIreVTLDSLRRAIGVV------P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 88 QGVhlhVL--ESIIVVLRAsgGRDNAqGRAQILAILEQLGITHLALQYLDQ-----------LSGGQRQLVGLAQSLIRR 154
Cdd:cd03253 82 QDT---VLfnDTIGYNIRY--GRPDA-TDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 155 PELLLLDEPLSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAPE 222
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRD--VSKGRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHE 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-224 |
2.79e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSlP--QGVHLHVLESIIVVLRAS 105
Cdd:PRK13635 32 EGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN-PdnQFVGATVQDDVAFGLENI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 G-GRDNAQGRAQilAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQ 184
Cdd:PRK13635 111 GvPREEMVERVD--QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1167959503 185 ARNRVTIVVAHDINIALRhGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK13635 189 QKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-228 |
3.35e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 61.39 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQK-VVF 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEV-PKGEVTCVLGRNGVGKTTLLKTLMGLLPVkSGSIRLDGEDITKLPPHERARAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQ---SLPQgvhLHVLESIIVVLRASGGRdnaqGRAQILAILEQLGITHlalQYLDQ----LSGGQRQLVGLAQSLIRR 154
Cdd:TIGR03410 80 VPQgreIFPR---LTVEENLLTGLAALPRR----SRKIPDEIYELFPVLK---EMLGRrggdLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 155 PELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-229 |
3.71e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKS-TLLRSL----AGLNNADGEALLDGEDLMSLSFaeRAQKVVFL---PQSLPQGVHL---HVL 95
Cdd:PRK10418 26 LQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAGRVLLDGKPVAPCAL--RGRKIATImqnPRSAFNPLHTmhtHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESiivvLRASGGRDNaqgRAQILAILEQLGI--THLALQ-YLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQ 172
Cdd:PRK10418 104 ET----CLALGKPAD---DATLTAALEAVGLenAARVLKlYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 173 FHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAER 229
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-233 |
5.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQKV--VFlpqslpQGVHLHVLESIIVVLR 103
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRKHIgiVF------QNPDNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNA----QGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLV 179
Cdd:PRK13648 106 AFGLENHAvpydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 180 RRDTQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAPETVIT-AERLAEV 233
Cdd:PRK13648 186 RKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIFDhAEELTRI 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-216 |
5.63e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 61.67 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQK-----VVFlpQ----SL-PQgvhLHVL 95
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTsGEILFDGQDITGLSGRELRPLrrrmqMVF--QdpyaSLnPR---MTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVVLRASGGRDNAQGRAQILAILEQLGithLALQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:COG4608 116 DIIAEPLRIHGLASKAERRERVAELLELVG---LRPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1167959503 172 QFHVMDLVrRDTQARNRVTIV-VAHDINIaLRH-GDHVLMLKDGRLV 216
Cdd:COG4608 193 QAQVLNLL-EDLQDELGLTYLfISHDLSV-VRHiSDRVAVMYLGKIV 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-199 |
6.12e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.84 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PR-GKITILLGPNGCGKSTLLRSLAG-----LNNADGEALLD-------GEDLMSL--SFAERAQKVVFLPQ---SLPQG 89
Cdd:cd03236 23 PReGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPPDWDeildefrGSELQNYftKLLEGDVKVIVKPQyvdLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 90 VHLHVLESIivvlrasggrDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDL 169
Cdd:cd03236 103 VKGKVGELL----------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|
gi 1167959503 170 NYQFHVMDLVRRDTQARNRVtIVVAHDINI 199
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYV-LVVEHDLAV 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-224 |
6.61e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGL---NNADGEALLDGEDLMSLSFAERAQK-VVFLPQSLPQGVHLHVLESIIV--VLR 103
Cdd:TIGR02633 27 GECVGLCGENGAGKSTLMKILSGVyphGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPELSVAENIFLgnEIT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNAQG---RAQILAILEQLGITHLALQYLDqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVr 180
Cdd:TIGR02633 107 LPGGRMAYNAmylRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDII- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1167959503 181 RDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:TIGR02633 185 RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-225 |
7.90e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 61.69 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEP-GEVLGVIGPSGSGKSTLARLLVGVwPPTAGSVRLDGADLSQWDREELGRHIGYLPQD- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pqgVHL---HVLESIIvvlRASGGRDNAQGRAQILAILEQLgITHLALQYlD--------QLSGGQRQLVGLAqsliRrp 155
Cdd:COG4618 415 ---VELfdgTIAENIA---RFGDADPEKVVAAAKLAGVHEM-ILRLPDGY-DtrigeggaRLSGGQRQRIGLA----R-- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 156 elllldeplsALDLNYQFHVMD-------------LVR--RDTQARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASGA 220
Cdd:COG4618 481 ----------ALYGDPRLVVLDepnsnlddegeaaLAAaiRALKARGATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGP 549
|
....*
gi 1167959503 221 PETVI 225
Cdd:COG4618 550 RDEVL 554
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-67 |
9.19e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.44 E-value: 9.19e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLN------NADGEALLDGEDL 67
Cdd:COG1117 14 VRNLNVYYGDKQALKDINLDI-PENKVTALIGPSGCGKSTLLRCLNRMNdlipgaRVEGEILLDGEDI 80
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-224 |
9.69e-11 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 60.54 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMS---LSFAERAQKV--VF-LPQSlpQGVHLHVLESIIV 100
Cdd:TIGR04521 29 EDGEFVAIIGHTGSGKSTLIQHLNGLLKPTsGTVTIDGRDITAkkkKKLKDLRKKVglVFqFPEH--QLFEETVYKDIAF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 VLRASG-GRDNAQGRAQilAILEQLGITHlalQYLDQ----LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHV 175
Cdd:TIGR04521 107 GPKNLGlSEEEAEERVK--EALELVGLDE---EYLERspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 176 MDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:TIGR04521 182 LDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-235 |
1.18e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.33 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgVHL-H 93
Cdd:COG1132 353 RPVLKDISL-TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTsGRILIDGVDIRDLTLESLRRQIGVVPQD----TFLfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 --VLESIivvlraSGGRDNAqGRAQILAILEQLGITHLALQyLDQ------------LSGGQRQLVGLAQSLIRRpelll 159
Cdd:COG1132 428 gtIRENI------RYGRPDA-TDEEVEEAAKAAQAHEFIEA-LPDgydtvvgergvnLSGGQRQRIAIARALLKDppili 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 160 ldeplSALDlnyqFHVMDLVRR--DTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITAERL-AEVYR 235
Cdd:COG1132 500 ldeatSALD----TETEALIQEalERLMKGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELLARGGLyARLYR 573
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-151 |
2.31e-10 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 58.38 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFA-ERAQKVVFLPQSLPqgv 90
Cdd:cd03268 10 YGKKRVLDDISLHV-KKGEIYGFLGPNGAGKTTTMKIILGLIKPDsGEITFDGKSYQKNIEAlRRIGALIEAPGFYP--- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 91 HLHVLESIIVVLRASGGRDNAQGRaqilaILEQLGITHLALQYLDQLSGGQRQLVGLAQSL 151
Cdd:cd03268 86 NLTARENLRLLARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALAL 141
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-219 |
2.37e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.78 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgVHLH-- 93
Cdd:cd03251 16 PVLRDISLDI-PAGETVALVGPSGSGKSTLVNLIPRFYDVDsGRILIDGHDVRDYTLASLRRQIGLVSQD----VFLFnd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 -VLESIIVvlrasgGRDNAqGRAQILAILEQLG----ITHLALQYlD--------QLSGGQRQLVGLAQSLIRRPELLLL 160
Cdd:cd03251 91 tVAENIAY------GRPGA-TREEVEEAARAANahefIMELPEGY-DtvigergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 161 DEPLSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASG 219
Cdd:cd03251 163 DEATSALDTESERLVQAALER--LMKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-219 |
2.46e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.88 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGED----------LMSLSFAERAQkvvf 81
Cdd:cd03267 31 YREVEALKGISFTI-EKGEIVGFIGPNGAGKTTTLKILSGLLQPTsGEVRVAGLVpwkrrkkflrRIGVVFGQKTQ---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSLPqgvhlhVLESIiVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:cd03267 106 LWWDLP------VIDSF-YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 162 EPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-214 |
3.07e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.25 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 10 SAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGlnnadgE-ALLDGEDLMSLSFAeraqkvvFLPQS--L 86
Cdd:cd03250 12 SGEQETSFTLKDINL-EVPKGELVAIVGPVGSGKSSLLSALLG------ElEKLSGSVSVPGSIA-------YVSQEpwI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQGVhlhVLESIIV-----------VLRASG-GRDnaqgraqiLAILEQL--------GIThlalqyldqLSGGQRQLVG 146
Cdd:cd03250 78 QNGT---IRENILFgkpfdeeryekVIKACAlEPD--------LEILPDGdlteigekGIN---------LSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 147 LAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIaLRHGDHVLMLKDGR 214
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-152 |
3.49e-10 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 59.68 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 3 GLMLRSFSAGYSTQPVIADLNVPLLPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVF 81
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSlpqgVHLH---VLESIIVvlrasgGRDNAQGrAQILAILEQLGITHLALQYLD-----------QLSGGQRQLVGL 147
Cdd:TIGR02868 414 CAQD----AHLFdttVRENLRL------ARPDATD-EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
....*
gi 1167959503 148 AQSLI 152
Cdd:TIGR02868 483 ARALL 487
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-227 |
4.48e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 59.28 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQslpqGVHLH- 93
Cdd:TIGR01842 331 KPTLRGISFSLQA-GEALAIIGPSGSGKSTLARLIVGIwPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ----DVELFp 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 --VLESIivvlraSGGRDNAQGRAQILAilEQLGITHLALQYLDQ------------LSGGQRQLVGLAQSLIRRPELLL 159
Cdd:TIGR01842 406 gtVAENI------ARFGENADPEKIIEA--AKLAGVHELILRLPDgydtvigpggatLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 160 LDEPLSALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAI-KALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-227 |
5.39e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 9 FSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNA------DGEALLDGEDLMSLSFAE----RAQK 78
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQI-EAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLHASEQTlrgvRGNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 79 VVFLPQ----SLPQgvhLHVLE-SIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLD---QLSGGQRQLVGLAQS 150
Cdd:PRK15134 94 IAMIFQepmvSLNP---LHTLEkQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 151 LIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-229 |
5.58e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERA---QKV--VFlpQ----SL-PQGVHLHVL 95
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETpTGGELYYQGQDLLKADPEAQKllrQKIqiVF--QnpygSLnPRKKVGQIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVV---LRAsggrdnAQGRAQILAILEQLGI-THLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:PRK11308 116 EEPLLIntsLSA------AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 172 QFHVMDLVrRDTQARNRVTIV-VAHDINIaLRH-GDHVLMLKDGRLVASGAPETVITAER 229
Cdd:PRK11308 190 QAQVLNLM-MDLQQELGLSYVfISHDLSV-VEHiADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-197 |
6.59e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEALldgedlmslsfaERAQKVVFLPQSLPQGVHLHVLEsiivVLRASGGR 108
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------DEDLKISYKPQYISPDYDGTVEE----FLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 DNAQGRAQILaILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNR 188
Cdd:COG1245 429 DFGSSYYKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
....*....
gi 1167959503 189 VTIVVAHDI 197
Cdd:COG1245 508 TAMVVDHDI 516
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-218 |
6.60e-10 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 56.28 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERaqkvvflpqslpqgvhlhvlesiivvlras 105
Cdd:cd03216 23 VRRGEVHALLGENGAGKSTLMKILSGLYKPDsGEILVDGKEVSFASPRDA------------------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 ggrdnaqgraqilailEQLGIthlALQYldQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdTQA 185
Cdd:cd03216 73 ----------------RRAGI---AMVY--QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR-LRA 130
|
170 180 190
....*....|....*....|....*....|...
gi 1167959503 186 RNRVTIVVAHDINIALRHGDHVLMLKDGRLVAS 218
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-154 |
6.66e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.92 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLLPRGKItILLGPNGCGKSTLLRSLAGLNNADgeallDGEdlmsLSFAERAqKVVFLPQSLPQGVHL 92
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRI-GLVGRNGAGKSTLLKILAGELEPD-----SGE----VSIPKGL-RIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 HVLEsiiVVLRASGGRDNAQGR----------------------------------AQILAILEQLGITHLAL-QYLDQL 137
Cdd:COG0488 77 TVLD---TVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEEDLdRPVSEL 153
|
170
....*....|....*..
gi 1167959503 138 SGGQRQLVGLAQSLIRR 154
Cdd:COG0488 154 SGGWRRRVALARALLSE 170
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-225 |
6.98e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 57.55 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLLPrGKITILLGPNGCGKST---LLRSLAGLNNadGEALLDGEDLMSLSFAERAQKVVFLPQSlPQGVHL 92
Cdd:cd03249 16 VPILKGLSLTIPP-GKTVALVGSSGCGKSTvvsLLERFYDPTS--GEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 HVLESIIVvlrasgGRDNAQ--------GRAQILAILEQL--GITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:cd03249 92 TIAENIRY------GKPDATdeeveeaaKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 163 PLSALDLNYQFHVMDLVrrDTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:cd03249 166 ATSALDAESEKLVQEAL--DRAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-230 |
7.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLESIIVVLRASG 106
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 GRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQAR 186
Cdd:PRK13652 108 GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1167959503 187 NRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERL 230
Cdd:PRK13652 188 GMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-153 |
1.33e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQKVVFLPQSL-PqgvHLHVLESIivvlrASGG 107
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWIGGRVVNELEPADRDIAMVFQNYALyP---HMSVRENM-----AYGL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 108 RDNAQGRAQILA-ILEQLGITHLAlQYLD----QLSGGQRQLVGLAQSLIR 153
Cdd:PRK11650 102 KIRGMPKAEIEErVAEAARILELE-PLLDrkprELSGGQRQRVAMGRAIVR 151
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-218 |
1.47e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAER-AQKVVFLPQSLPQGVHLHVLESIIV-VLRAS 105
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPDaGSILIDGQEMRFASTTAAlAAGVAIIYQELHLVPEMTVAENLYLgQLPHK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGR-DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdTQ 184
Cdd:PRK11288 109 GGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRE-LR 187
|
170 180 190
....*....|....*....|....*....|....
gi 1167959503 185 ARNRVTIVVAHDINIALRHGDHVLMLKDGRLVAS 218
Cdd:PRK11288 188 AEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-213 |
1.50e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 9 FSAGySTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL------------NNADGEALLDGEDLMSLSFAERA 76
Cdd:cd03290 8 FSWG-SGLATLSNINIRI-PTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwsnKNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 77 QKVVFLPQSLPQGVhlhVLESIIVVLRASGGRD--NAQGRAQILAILEQLGITHLALQyldqLSGGQRQLVGLAQSLIRR 154
Cdd:cd03290 86 QKPWLLNATVEENI---TFGSPFNKQRYKAVTDacSLQPDIDLLPFGDQTEIGERGIN----LSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 155 PELLLLDEPLSALDLNYQFHVMDL-VRRDTQARNRVTIVVAHDINIaLRHGDHVLMLKDG 213
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-224 |
1.94e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLM-------SLSFAERAQ------KVVFLPQSLPQGVHLHVL 95
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTINlvrdkdgQLKVADKNQlrllrtRLTMVFQHFNLWSHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVVLRASGGRDNAQGRAQILAILEQLGITHLA-LQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFH 174
Cdd:PRK10619 111 ENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 175 VMDLVRRDTQaRNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK10619 191 VLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-226 |
2.58e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.20 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLLpRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDG----------EDLMSLSFAER 75
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIY-QSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqniyERRVNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 76 AQKVVF-LPQSLPQGVHLHVLESIIVVlrasGGRDNaqgraqilaiLEQLGITHLALQYLD--------------QLSGG 140
Cdd:PRK14258 89 QVSMVHpKPNLFPMSVYDNVAYGVKIV----GWRPK----------LEIDDIVESALKDADlwdeikhkihksalDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 141 QRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIV-VAHDINIALRHGDHVLMLKD-----GR 214
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLI-QSLRLRSELTMViVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250
....*....|..
gi 1167959503 215 LVASGAPETVIT 226
Cdd:PRK14258 234 LVEFGLTKKIFN 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-208 |
2.58e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 56.26 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDlmslsfaeraqkVVFLPQSLP---QGVHLHVLESIIvvlra 104
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGvLKPDEGDIEIELDT------------VSYKPQYIKadyEGTVRDLLSSIT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 105 sggrDNAQGRAQ-ILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDT 183
Cdd:cd03237 87 ----KDFYTHPYfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*
gi 1167959503 184 QARNRVTIVVAHDINIALRHGDHVL 208
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-225 |
3.55e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 56.67 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTqPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSl 86
Cdd:TIGR01193 480 SYSYGYGS-NILSDISLTIKMNSKTTIV-GMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQE- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 PQGVHLHVLESIIVVLRASGGRDN---AQGRAQILAILEQLGI---THLALQYLDqLSGGQRQLVGLAQSLIRRPELLLL 160
Cdd:TIGR01193 557 PYIFSGSILENLLLGAKENVSQDEiwaACEIAEIKDDIENMPLgyqTELSEEGSS-ISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 161 DEPLSALDLNYQFHVMD-LVRrdtqARNRVTIVVAHDINIALRhGDHVLMLKDGRLVASGAPETVI 225
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNnLLN----LQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-222 |
4.55e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.84 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNN---ADGEALLDGEDLMSLSFAERAQKVVFL-PQSLP--QGVhlhvleSIIVVLR 103
Cdd:cd03217 26 GEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGEDITDLPPEERARLGIFLaFQYPPeiPGV------KNADFLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 asggrdnaqgraqilaileqlgithlalqYLDQ-LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRd 182
Cdd:cd03217 100 -----------------------------YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1167959503 183 TQARNRVTIVVAHDINIA-LRHGDHVLMLKDGRLVASGAPE 222
Cdd:cd03217 150 LREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-219 |
5.36e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPR-GKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLSFAERAQ-KVVFLPQSLPQGVHLH 93
Cdd:PRK09700 17 PVHALKSVNLTVYpGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLDHKLAAQlGIGIIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIIVvlrasgGR------------DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:PRK09700 97 VLENLYI------GRhltkkvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 162 EPLSAL---DLNYQFHVMDLVRRDTQArnrvTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:PRK09700 171 EPTSSLtnkEVDYLFLIMNQLRKEGTA----IVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
35-231 |
5.74e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 35 LLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKV--VFLPQSLPQGVHLHVLESIIVVLRASGGRDNA 111
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMiEPTSGELLIDDHPLHFGDYSYRSQRIrmIFQDPSTSLNPRQRISQILDFPLRLNTDLEPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 112 QGRAQILAILEQLGI-THLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVT 190
Cdd:PRK15112 124 QREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1167959503 191 IVVAHDINIALRHGDHVLMLKDGRLVASGApetviTAERLA 231
Cdd:PRK15112 204 IYVTQHLGMMKHISDQVLVMHQGEVVERGS-----TADVLA 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-227 |
6.73e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLS------FAERAQkVVFLPQSLPQGVHLHVLESIIV 100
Cdd:PRK15134 309 LRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNrrqllpVRHRIQ-VVFQDPNSSLNPRLNVLQIIEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 101 VLRASGGRDNAQGR-AQILAILEQLGITHLALQ-YLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDL 178
Cdd:PRK15134 388 GLRVHQPTLSAAQReQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILAL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 179 VRRDTQARNRVTIVVAHDINI--ALRHgdHVLMLKDGRLVASGAPETVITA 227
Cdd:PRK15134 468 LKSLQQKHQLAYLFISHDLHVvrALCH--QVIVLRQGEVVEQGDCERVFAA 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-199 |
9.19e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 25 PLLPRGKITILLGPNGCGKSTLLRSLAG-----LNNADGEALLDG--------------EDLmslsfAERAQKVVFLPQs 85
Cdd:PRK13409 94 PIPKEGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEPSWDEvlkrfrgtelqnyfKKL-----YNGEIKVVHKPQ- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 86 lpqgvhlhVLESIIVVLRASGGR--DNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:PRK13409 168 --------YVDLIPKVFKGKVREllKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*.
gi 1167959503 164 LSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINI 199
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRE--LAEGKYVLVVEHDLAV 273
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-222 |
1.50e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 7 RSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNA-DGE--------ALLDGEDLMSLsfaeRAQ 77
Cdd:PRK10535 12 RSYPSGEEQVEVLKGISLDIYA-GEMVAIVGASGSGKSTLMNILGCLDKPtSGTyrvagqdvATLDADALAQL----RRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVVFLPQSLPQGVHLHVLESI-IVVLRASGGRDNAQGRAQilAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPE 156
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVeVPAVYAGLERKQRLLRAQ--ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 157 LLLLDEPLSALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINIAlRHGDHVLMLKDGRLVASGAPE 222
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQ 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-224 |
1.69e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGE-----------DLMSLSFAERAQKVVF 81
Cdd:PRK14267 14 YGSNHVIKGVDL-KIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlfgrniyspDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSLPqgvHLHVLESIIVVLRASGgrdNAQGRAQILAILEqLGITHLAL---------QYLDQLSGGQRQLVGLAQSLI 152
Cdd:PRK14267 93 YPNPFP---HLTIYDNVAIGVKLNG---LVKSKKELDERVE-WALKKAALwdevkdrlnDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 153 RRPELLLLDEPLSALDLNYQFHVMDLVrrdTQARNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELL---FELKKEYTIVlVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-222 |
2.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKV--VFlpqslpQGVHLHVLESIIVVLR 103
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrGRVKVMGREVNAENEKWVRSKVglVF------QDPDDQVFSSTVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNAQGRAQIL----AILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLV 179
Cdd:PRK13647 102 AFGPVNMGLDKDEVErrveEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1167959503 180 RRdTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPE 222
Cdd:PRK13647 182 DR-LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-225 |
2.22e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.42 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAG-LNNADGEA-LLDGE---DLMSLSFAERA---QKVVFLPQSLPQGVHLHVLESIIVV 101
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGvLEPTSGEVnVRVGDewvDMTKPGPDGRGrakRYIGILHQEYDLYPHRTVLDNLTEA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 LRASGGRDNAQGRAQIlaILEQLGIT-----HLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVM 176
Cdd:TIGR03269 390 IGLELPDELARMKAVI--TLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 177 DLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:TIGR03269 468 HSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-218 |
2.33e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGL---NNADGEALLDGEDLMSLSFAERAQK-VVFLPQSLPQGVHL 92
Cdd:PRK13549 18 VKALDNVSLkVRAGEIVSLCGENGAGKSTLMKVLSGVyphGTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 HVLESI-----IVvlraSGGR---DNAQGRAQILaiLEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:PRK13549 98 SVLENIflgneIT----PGGImdyDAMYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 165 SALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVAS 218
Cdd:PRK13549 172 ASLTESETAVLLDII-RDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-224 |
3.08e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 37 GPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAERAQK-----VVF---LPQSLPQgvhLHVLESIIVVLRASGG 107
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKAtDGEVAWLGKDLLGMKDDEWRAVrsdiqMIFqdpLASLNPR---MTIGEIIAEPLRTYHP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 108 R-DNAQGRAQILAILEQLGI-THLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQA 185
Cdd:PRK15079 131 KlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRE 210
|
170 180 190
....*....|....*....|....*....|....*....
gi 1167959503 186 RNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK15079 211 MGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-216 |
3.11e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGEDLMSLS-----FAERAQKVVFLPQSLPQGVHLHVLESIIVVLR 103
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDITRLKnrevpFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNaqgRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrrdt 183
Cdd:PRK10908 108 GASGDDI---RRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLF---- 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1167959503 184 QARNRVTIVV---AHDINIALRHGDHVLMLKDGRLV 216
Cdd:PRK10908 181 EEFNRVGVTVlmaTHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-230 |
4.34e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 52.49 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALLDGEDLMSLSFAE-RAQKVVFLPQSLpqgvhlhVL 95
Cdd:cd03252 17 ILDNISLRIKP-GEVVGIVGRSGSGKSTLTKLIQRFYVPeNGRVLVDGHDLALADPAWlRRQVGVVLQENV-------LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVVLRASGgrDNAQGRAQILAILEQLG----ITHLALQYlDQ--------LSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:cd03252 89 NRSIRDNIALA--DPGMSMERVIEAAKLAGahdfISELPEGY-DTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 164 LSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITAERL 230
Cdd:cd03252 166 TSALDYESEHAIMRNMHD--ICAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-168 |
5.93e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPRGkITILLGPNGCGKSTLLRSLAGLNNAD------GEALLDGEDLmslsFAERAQ 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNE-ITALIGPSGSGKSTLLRSINRMNDLNpevtitGSIVYNGHNI----YSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KV--------VFL-PQSLPQGVHlhvlESIIVVLRASGGRDNAQGRAQILAILEQLGITHLALQYLDQ----LSGGQRQL 144
Cdd:PRK14239 81 TVdlrkeigmVFQqPNPFPMSIY----ENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQR 156
|
170 180
....*....|....*....|....
gi 1167959503 145 VGLAQSLIRRPELLLLDEPLSALD 168
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-225 |
8.92e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAqKVVFLPQ 84
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVAS-GECFGLLGPNGAGKSTIARMILGMTSPDaGKITVLGVPVPARARLARA-RIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 SLPQGVHLHVLESIIVVLRASGgRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 165 SALDLNYQfHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:PRK13536 201 TGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-221 |
9.09e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 51.34 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQS--LPQGV-- 90
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIV-GRTGSGKSSLLLALFRLvELSSGSILIDGVDISKIGLHDLRSRISIIPQDpvLFSGTir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 ------HLHVLESIIVVLRasggrdnaqgRAQILAILEQLGITHLALQYLD--QLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:cd03244 96 snldpfGEYSDEELWQALE----------RVGLKEFVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 163 PLSALDLNYQFHVMDLVRrdTQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAP 221
Cdd:cd03244 166 ATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTII-DSDRILVLDKGRVVEFDSP 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-197 |
1.63e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEALldgedlmslsfaERAQKVVFLPQSLPQGVHLHVLEsiivVLRASGGR 108
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------------DPELKISYKPQYIKPDYDGTVED----LLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 -DNAQGRAQILailEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARN 187
Cdd:PRK13409 428 lGSSYYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
170
....*....|
gi 1167959503 188 RVTIVVAHDI 197
Cdd:PRK13409 505 ATALVVDHDI 514
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-200 |
1.65e-07 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 50.43 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSfAERAQKVVFLPQSLPQGVHLHVLESIIVVLRASGGR 108
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPELSALENLHFWAAIHGGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 109 DNAqgraqILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNR 188
Cdd:TIGR01189 105 QRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGI 179
|
170
....*....|..
gi 1167959503 189 VTIVVAHDINIA 200
Cdd:TIGR01189 180 VLLTTHQDLGLV 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
1.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 5 MLRSFSAGYS---TQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVV 80
Cdd:PRK13644 1 MIRLENVSYSypdGTPALENINL-VIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 81 FLPQSLP--QGVHLHVLESIivvlraSGGRDN-----AQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIR 153
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDL------AFGPENlclppIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVRRdTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-228 |
1.98e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgvhlHVL 95
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVV-GRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQS-------PVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVVLRAS-------GGRDNAQGRAQILAILEQ--LGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSA 166
Cdd:PLN03232 1322 FSGTVRFNIDpfsehndADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 167 LDLNYQFHVMDLVRRdtQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:PLN03232 1402 VDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTII-DCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-227 |
2.03e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLN-NADGEALLDGEDLMSLSFAERAQKVVFLPQS--LPQGVHLHV 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIV-GRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDLRFKITIIPQDpvLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 95 LESIivvlraSGGRDNAQGRAQILAILEQL------GITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALD 168
Cdd:TIGR00957 1380 LDPF------SQYSDEEVWWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 169 LNYQFHVMDLVRrdTQARNRVTIVVAHDINIALRHgDHVLMLKDGRLVASGAPETVITA 227
Cdd:TIGR00957 1454 LETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-229 |
2.52e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADG----EAL-LDGEDLMSLSFAERAQKV------VFLPQSLPQGVHLHVLES 97
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLeFNGQDLQRISEKERRNLVgaevamIFQDPMTSLNPCYTVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 98 IIVVLRASGGRDNAQGRAQILAILEQLGITHLALQ---YLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFH 174
Cdd:PRK11022 112 IMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQ 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 175 VMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAER 229
Cdd:PRK11022 192 IIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-200 |
2.76e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 49.80 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmslsfaerAQKVVFLPQSLPQGVHLHVLESIIVVLRAS 105
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLLNGGPL--------DFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQA 185
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
170
....*....|....*
gi 1167959503 186 RNRVTIVVAHDINIA 200
Cdd:cd03231 175 GGMVVLTTHQDLGLS 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-142 |
3.29e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.83 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLnnadgEALLDGEdlmsLSFAERAqKVVFLP 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSL-RIDRGDRIGLIGPNGAGKSTLLKLLAGE-----LEPDSGT----VKLGETV-KIGYFD 384
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 84 QSLPQgvhLHVLESIIVVLRasGGRDNAQgRAQILAILEQLGIT-HLALQYLDQLSGGQR 142
Cdd:COG0488 385 QHQEE---LDPDKTVLDELR--DGAPGGT-EQEVRGYLGRFLFSgDDAFKPVGVLSGGEK 438
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-224 |
4.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 5 MLRSFSAGYSTQP-------VIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQ 77
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfasrALFDIDLEV-KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 K-------VVF-LPQSlpqgvhlHVLESIIVVLRASGGRDNAQGRAQILAIL-EQLGITHLALQYLD----QLSGGQRQL 144
Cdd:PRK13643 80 KpvrkkvgVVFqFPES-------QLFEETVLKDVAFGPQNFGIPKEKAEKIAaEKLEMVGLADEFWEkspfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 145 VGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQArNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
35-222 |
4.99e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 35 LLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlP--QGVHLHVLESIIVVLRaSGGRDNA 111
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIGMVFQN-PdnQFVGATVEDDVAFGLE-NKGIPHE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 112 QGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTI 191
Cdd:PRK13650 116 EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVI 195
|
170 180 190
....*....|....*....|....*....|..
gi 1167959503 192 VVAHDIN-IALrhGDHVLMLKDGRLVASGAPE 222
Cdd:PRK13650 196 SITHDLDeVAL--SDRVLVMKNGQVESTSTPR 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-233 |
5.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQKVVFLPQSLPQGVHLHVLESIIvvlrAS 105
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDV----AF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGRDNAQGRAQILAILEQlgiTHLALQYLD-------QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDL 178
Cdd:PRK13642 106 GMENQGIPREEMIKRVDE---ALLAVNMLDfktrepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 179 VRRDTQARNRVTIVVAHDINIALRhGDHVLMLKDGRLVASGAP-ETVITAERLAEV 233
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPsELFATSEDMVEI 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
5.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGEDLM--SLSFAERAQKVVFLPQSLPQGVHLHVLESIIVVLRAS 105
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 106 GGRDNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrRDTQA 185
Cdd:PRK13639 107 LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1167959503 186 RNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-152 |
5.37e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.72 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAqkvVFLPQSLPQGVHLHVLESIIVVLRASGGR 108
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLlPPAAGTIKLDGGDIDDPDVAEAC---HYLGHRNAMKPALTVAENLEFWAAFLGGE 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1167959503 109 DnaqgrAQILAILEQLG---ITHLALQYldqLSGGQRQLVGLAQSLI 152
Cdd:PRK13539 105 E-----LDIAAALEAVGlapLAHLPFGY---LSAGQKRRVALARLLV 143
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-230 |
5.75e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 50.23 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKVVFLPQSlPQGVHLHVLESIIVvlrasg 106
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQN-PQLPHGTLRDNVLL------ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 107 GRDNAqGRAQILAILEQLGITH--------LALQYLDQ---LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHV 175
Cdd:PRK11174 446 GNPDA-SDEQLQQALENAWVSEflpllpqgLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 176 MDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITAERL 230
Cdd:PRK11174 525 MQALNA--ASRRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
31-230 |
6.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 31 KITILLGPNGCGKSTLLRSLAGLNNADGEALLDGE-----DLMSLSFAERAQKVVFLPQSLPQ-GVHLHVLESIIVVLRA 104
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipaNLKKIKEVKRLRKEIGLVFQFPEyQLFQETIEKDIAFGPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 105 SGGRDNAQGRAQILAILEqlgITHLALQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVR 180
Cdd:PRK13645 118 NLGENKQEAYKKVPELLK---LVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 181 RDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERL 230
Cdd:PRK13645 195 RLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-51 |
6.87e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.23 E-value: 6.87e-07
10 20 30
....*....|....*....|....*....|...
gi 1167959503 19 IADLNVPLLPRGKITILLGPNGCGKSTLLRSLA 51
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-87 |
8.83e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 8.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 16 QPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNN---ADGEALLDGEDLMSLSFAERAQKVVFLPQSLP 87
Cdd:PRK09580 14 KAILRGLNLEVRP-GEVHAIMGPNGSGKSTLSATLAGREDyevTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYP 87
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-151 |
1.19e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 10 SAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLmSLSFAER------AQKVVFlp 83
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKL-PPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-KLAYVDQsrdaldPNKTVW-- 404
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 84 QSLPQGVHLHVLESIIVVLRASGGRDNAQGRAQilaileQlgithlalQYLDQLSGGQRQLVGLAQSL 151
Cdd:TIGR03719 405 EEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQ------Q--------KKVGQLSGGERNRVHLAKTL 458
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-221 |
1.35e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 47.79 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQ--SLPQGVhlh 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIV-GRTGAGKSTLILALFRFLEAEeGKIEIDGIDISTIPLEDLRSSLTIIPQdpTLFSGT--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 vlesiivvLRASGGRDNAQGRAQILAILEqlgITHLALQyldqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQF 173
Cdd:cd03369 98 --------IRSNLDPFDEYSDEEIYGALR---VSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1167959503 174 HVMDLVRRDTQarNRVTIVVAHDINIALRHgDHVLMLKDGRLVASGAP 221
Cdd:cd03369 163 LIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-219 |
1.46e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 8 SFSAGYSTQPViADLNVPLLPrGKITILLGPNGCGKSTLLRSLA-GLNNADGEALLDGEDLMSLSFA--ERAQKVVFLPQ 84
Cdd:PRK13657 341 SFSYDNSRQGV-EDVSFEAKP-GQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 85 SLpqgvhlhVLESIIVVLRAsgGRDNAQ--------GRAQILAILEQ--LGITHLALQYLDQLSGGQRQLVGLAQSLIRR 154
Cdd:PRK13657 419 GL-------FNRSIEDNIRV--GRPDATdeemraaaERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 155 PELLLLDEPLSALDLNYQFHVMDLVrrDTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASG 219
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAAL--DELMKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-149 |
1.68e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEdlmSLSFAERAQKVVFLPQSLPQGVHLHVL 95
Cdd:PRK13543 25 PVFGPLDFHVDA-GEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGK---TATRGDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 96 ESiIVVLRASGGRDNAQGRAQILAIleqLGITHLALQYLDQLSGGQRQLVGLAQ 149
Cdd:PRK13543 101 EN-LHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALAR 150
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-224 |
1.73e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPLlPRGKITILLGPNGCGKSTLLRSLAGL--NNA--DGEALLDGEDLMSLSFAE----RAQKVVFLPQ----SL-P 87
Cdd:PRK09473 34 DLNFSL-RAGETLGIVGESGSGKSQTAFALMGLlaANGriGGSATFNGREILNLPEKElnklRAEQISMIFQdpmtSLnP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 88 qgvHLHVLESIIVVLRASGGRDNAQGRAQILAILEQLGITHlALQ----YLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:PRK09473 113 ---YMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 164 LSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-219 |
1.73e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVpLLPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALldgedlmslsfAERAqkVVFLPQSlPQGVHLHVLESII 99
Cdd:PTZ00243 678 DVSV-SVPRGKLTVVLGATGSGKSTLLQSLLSqFEISEGRVW-----------AERS--IAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 100 VVLRASGGR-DNAQGRAQILAILEQLGI---THLALQYLDqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLnyqfHV 175
Cdd:PTZ00243 743 FFDEEDAARlADAVRVSQLEADLAQLGGgleTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDA----HV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1167959503 176 MDLVRRDT---QARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASG 219
Cdd:PTZ00243 818 GERVVEECflgALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSG 863
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
121-232 |
1.77e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.31 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 121 LEQLGithLALQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIVVAHD 196
Cdd:PRK13631 160 LNKMG---LDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHT 235
|
90 100 110
....*....|....*....|....*....|....*.
gi 1167959503 197 INIALRHGDHVLMLKDGRLVASGAPETVITAERLAE 232
Cdd:PRK13631 236 MEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-225 |
2.01e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgVHLH---VLESIivvl 102
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKSTIANLLTRFYDIDeGEILLDGHDLRDYTLASLRNQVALVSQN----VHLFndtIANNI---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 103 raSGGRDNAQGRAQIlailEQLGITHLALQYLDQ---------------LSGGQRQLVGLAQSLIRRPELLLLDEPLSAL 167
Cdd:PRK11176 438 --AYARTEQYSREQI----EEAARMAYAMDFINKmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167959503 168 DLNYQFHVMDLVrrDTQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:PRK11176 512 DTESERAIQAAL--DELQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-149 |
2.39e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 18 VIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDlmslsfaeraQKVVFLPQSlPQGVHLHVLES 97
Cdd:TIGR00954 467 LIESLSFEV-PSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK----------GKLFYVPQR-PYMTLGTLRDQ 534
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 98 IIVVLRASGGRDNAQGRAQILAILEQLGITHL--------ALQ-YLDQLSGGQRQLVGLAQ 149
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHIlereggwsAVQdWMDVLSGGEKQRIAMAR 595
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-153 |
2.48e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFL 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHA-GEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 83 pqsLPQGVHL----HVLESIIvvLRASGGRDNAQGRAQILAileQLGiTHLALQYL-DQLSGGQRQLVGLAQSLIR 153
Cdd:PRK15439 91 ---VPQEPLLfpnlSVKENIL--FGLPKRQASMQKMKQLLA---ALG-CQLDLDSSaGSLEVADRQIVEILRGLMR 157
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-52 |
2.72e-06 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 45.90 E-value: 2.72e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPRGKItILLGPNGCGKSTLLRSLAG 52
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRI-GLVGRNGAGKSTLLKLIAG 48
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-219 |
2.95e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAE-----RAQKVVFLPQSLPQGVHLHVLESIIVVLR 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDPYASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 ASGGRDNAQGRAQILAILEQLGIT-HLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRD 182
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190
....*....|....*....|....*....|....*..
gi 1167959503 183 TQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-82 |
2.95e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAG---LNNADGEALLDGEDLMSLSFAERAQKVV 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSI-NKGEIHAIMGPNGSGKSTLSKVIAGhpaYKILEGDILFKGESILDLEPEERAHLGI 86
|
..
gi 1167959503 81 FL 82
Cdd:CHL00131 87 FL 88
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
3.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVpLLPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSlsfAERAQK----------VVF-LPQSlpQG 89
Cdd:PRK13634 25 DVNV-SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT---AGKKNKklkplrkkvgIVFqFPEH--QL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 90 VHLHVLESIivvlrASG------GRDNAQGRAQilAILEQLGITHlalQYLDQ----LSGGQRQLVGLAQSLIRRPELLL 159
Cdd:PRK13634 99 FEETVEKDI-----CFGpmnfgvSEEDAKQKAR--EMIELVGLPE---ELLARspfeLSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 160 LDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT-AERLAE 232
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdPDELEA 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-199 |
3.14e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 23 NVPLLPRGKITILLGPNGCGKSTLLRSLAG-----LNNADGEA--------------------LLDGEdlmsLSFAERAQ 77
Cdd:COG1245 92 GLPVPKKGKVTGILGPNGIGKSTALKILSGelkpnLGDYDEEPswdevlkrfrgtelqdyfkkLANGE----IKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVVFLPQSLpQGVHLHVLEsiivvlrasggrdNAQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPEL 157
Cdd:COG1245 168 YVDLIPKVF-KGTVRELLE-------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1167959503 158 LLLDEPLSALDLNYQFHVMDLVRRDTQArNRVTIVVAHDINI 199
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAI 274
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-222 |
3.55e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 47.73 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNNAD----GEALLDGE----DLMSLSFAERAQKVVFLPqslpqgvHLHVLESIIVV 101
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgsGSVLLNGMpidaKEMRAISAYVQQDDLFIP-------TLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 LRASGGRDNA--QGRAQILAILEQLGIT---HLALQYLDQ---LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQF 173
Cdd:TIGR00955 124 AHLRMPRRVTkkEKRERVDEVLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 174 HVMDLVRRDTQaRNRVTIVVAHDINIAL-RHGDHVLMLKDGRLVASGAPE 222
Cdd:TIGR00955 204 SVVQVLKGLAQ-KGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPD 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-221 |
3.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMS------LSFAERAQKVVF-LPQSlpQGVHLHVLESI 98
Cdd:PRK13646 30 FEQGKYYAIVGQTGSGKSTLIQNINALlKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFqFPES--QLFEDTVEREI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IVVLRASG-GRDNAQGRAQILaiLEQLGITHLALQYLD-QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVM 176
Cdd:PRK13646 108 IFGPKNFKmNLDEVKNYAHRL--LMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1167959503 177 DLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAP 221
Cdd:PRK13646 186 RLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-224 |
5.41e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 21 DLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-------GEALLDGEDLMSLSFAERAQKVVFLPQSL-PqgvH 91
Cdd:PRK11144 14 CLTVNLtLPAQGITAIFGRSGAGKTSLINAISGLTRPQkgrivlnGRVLFDAEKGICLPPEKRRIGYVFQDARLfP---H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVlesiivvlrasggRDN------AQGRAQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:PRK11144 91 YKV-------------RGNlrygmaKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 166 ALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-219 |
6.73e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.07 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGE-----DLMSLSFAERAQ 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYP-GEVLGIVGESGSGKTTLLNALSARLAPDaGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVV----FLPQSLPQGVHLHVLESIIVV--LRASGGRDNAQGRAQILAILEQLGIthlALQYLDQL----SGGQRQLVGL 147
Cdd:PRK11701 86 LLRtewgFVHQHPRDGLRMQVSAGGNIGerLMAVGARHYGDIRATAGDWLERVEI---DAARIDDLpttfSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167959503 148 AQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-219 |
7.50e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.33 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNA----DGEALLDGEDlmSLSFAERAQ-KVVFLPQsl 86
Cdd:cd03233 16 GRSKIPILKDFSGVVKP-GEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYNGIP--YKEFAEKYPgEIIYVSE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 87 pQGVHLHVL---ESIIVVLRASGGrdnaqgraqilaileqlgithlalQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEP 163
Cdd:cd03233 91 -EDVHFPTLtvrETLDFALRCKGN------------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 164 LSALDLNYQFHVMDLVRRDTQARNRVTIVV---AHDINIALRhgDHVLMLKDGRLVASG 219
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-227 |
8.82e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSlsfaERAQKVVFL-PQSLPQGVHLH------------ 93
Cdd:PRK10261 39 LQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR----RRSRQVIELsEQSAAQMRHVRgadmamifqepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 --------VLESIIVVLRASGGRDNAQGRAQILAILEQLGITH---LALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:PRK10261 115 tslnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 163 PLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVITA 227
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-229 |
8.90e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAERAQKVVFLPQSlPqgvhlhVL 95
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIV-GRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQA-P------VL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 96 ESIIVvlRASGGRDNAQGRAQILAILEQ-----------LGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPL 164
Cdd:PLN03130 1325 FSGTV--RFNLDPFNEHNDADLWESLERahlkdvirrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 165 SALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAPETVITAER 229
Cdd:PLN03130 1403 AAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTII-DCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-180 |
9.30e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 44.84 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVpLLPRGKITILLGPNGCGKSTLLRSLAGL-NNADGealldgedlmSLSFAERAQkVVFLPQS--LPQGVhl 92
Cdd:cd03223 14 RVLLKDLSF-EIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG----------RIGMPEGED-LLFLPQRpyLPLGT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 hvlesiivvLRasggrdnaqgraqilailEQLgithlALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQ 172
Cdd:cd03223 80 ---------LR------------------EQL-----IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
....*...
gi 1167959503 173 FHVMDLVR 180
Cdd:cd03223 128 DRLYQLLK 135
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-195 |
9.69e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 45.23 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 12 GYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNA---DGEALLDGEDLMSLSFAERaqkVVFLPQslpq 88
Cdd:cd03213 18 SKSGKQLLKNVSGKAKP-GELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGRPLDKRSFRKI---IGYVPQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 89 gvHLHVLESIIVvlrasggrdnaqgraqilaileqlgitHLALQY---LDQLSGGQRQLVGLAQSLIRRPELLLLDEPLS 165
Cdd:cd03213 90 --DDILHPTLTV---------------------------RETLMFaakLRGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190
....*....|....*....|....*....|
gi 1167959503 166 ALDLNYQFHVMDLVRRDTQaRNRVTIVVAH 195
Cdd:cd03213 141 GLDSSSALQVMSLLRRLAD-TGRTIICSIH 169
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-66 |
1.33e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 1.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1167959503 19 IADLNVPLLPrgKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGED 66
Cdd:COG3593 14 IKDLSIELSD--DLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEED 59
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-62 |
1.48e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.70 E-value: 1.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1167959503 17 PVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGLN-NADGEALL 62
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMAGVDkDFNGEARP 64
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-226 |
2.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLM----SLSFAERAQKV--VF-LPQSlpQGVHLHVLESI 98
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLMQHFNALlKPSSGTITIAGYHITpetgNKNLKKLRKKVslVFqFPEA--QLFENTVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 99 IVVLRASGGRDNaQGRAQILAILEQLGI-THLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMD 177
Cdd:PRK13641 108 EFGPKNFGFSED-EAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1167959503 178 LVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVIT 226
Cdd:PRK13641 187 LF-KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-220 |
2.80e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.32 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGedlmslSFAERAQKVVFLPQSLPQGVHL-HVLESiivvlra 104
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMKG------SVAYVPQQAWIQNDSLRENILFgKALNE------- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 105 sggrDNAQGRAQILAILEQLGI------THLALQYLDqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMD- 177
Cdd:TIGR00957 728 ----KYYQQVLEACALLPDLEIlpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEh 802
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1167959503 178 LVRRDTQARNRVTIVVAHDINIaLRHGDHVLMLKDGRLVASGA 220
Cdd:TIGR00957 803 VIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGS 844
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-62 |
3.18e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 3.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1167959503 17 PVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAGL-NNADGEALL 62
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMAGVdKEFEGEARP 66
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-53 |
3.39e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 3.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPLLPRGkITILLGPNGCGKSTLLRSLAGL 53
Cdd:PRK13541 11 IEQKNLFDLSITFLPSA-ITYIKGANGCGKSSLLRMIAGI 49
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-205 |
3.84e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 23 NVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNN------ADGEALLDGEDLMS-----LSFAERAQKVVFLPQSLPQGV 90
Cdd:PRK14243 28 NVWLdIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfrVEGKVTFHGKNLYApdvdpVEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 HlhvlESIIVVLRASGGR---DNAQGRAQILAIL-----EQLGITHLALqyldqlSGGQRQLVGLAQSLIRRPELLLLDE 162
Cdd:PRK14243 108 Y----DNIAYGARINGYKgdmDELVERSLRQAALwdevkDKLKQSGLSL------SGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1167959503 163 PLSALDLNYQFHVMDLVRrdtQARNRVTIV-VAHDINIALRHGD 205
Cdd:PRK14243 178 PCSALDPISTLRIEELMH---ELKEQYTIIiVTHNMQQAARVSD 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-219 |
4.73e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 43.29 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 1 MRGLMLRSFSAGYSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAeraqkV 79
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEV-PRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGRVSSLLGLG-----G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 80 VFLPQslpqgvhLHVLESIIVVLRASgGRDNAQGRAQILAILE--QLGithlalQYLDQ----LSGGQRQLVGLAQSLIR 153
Cdd:cd03220 94 GFNPE-------LTGRENIYLNGRLL-GLSRKEIDEKIDEIIEfsELG------DFIDLpvktYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167959503 154 RPELLLLDEPLSALDLNYQFHVMDLVrRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASG 219
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-52 |
6.16e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 6.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPRGKITILlGPNGCGKSTLLRSLAG 52
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAII-GENGVGKTTLLRTLVG 367
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-212 |
8.76e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 8.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 136 QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDINiALRHGDHVLMLKD 212
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-151 |
9.96e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 20 ADLNV-PllprGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDlmsLSF----AERAQKVVFLPQSLPQGVHLH 93
Cdd:PRK10762 23 AALNVyP----GRVMALVGENGAGKSTMMKVLTGIYTRDaGSILYLGKE---VTFngpkSSQEAGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 94 VLESIIVvlrasgGRD--NAQGR-------AQILAILEQLGITHLALQYLDQLSGGQRQLVGLAQSL 151
Cdd:PRK10762 96 IAENIFL------GREfvNRFGRidwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-91 |
2.25e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 2.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEA--LLDGEDLMSLSFAERAQKVVFLPQSLPQGVH 91
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviYIDGEDILEEVLDQLLLIIVGGKKASGSGEL 65
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-232 |
2.39e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 17 PVIADLNVPL-LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE-RAQKVvflpqslpqG-VHL 92
Cdd:COG3845 17 GVVANDDVSLtVRPGEIHALLGENGAGKSTLMKILYGLYQPDsGEILIDGKPVRIRSPRDaIALGI---------GmVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 93 H--------VLESIIVVLRASGGR--DNAQGRAQILAILEQLGithLAL---QYLDQLSGGQRQLVGLAQSLIRRPELLL 159
Cdd:COG3845 88 HfmlvpnltVAENIVLGLEPTKGGrlDRKAARARIRELSERYG---LDVdpdAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 160 ldeplsaLD-----LNYQ-----FHVMDLVRRDtqarnRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETViTAE 228
Cdd:COG3845 165 -------LDeptavLTPQeadelFEILRRLAAE-----GKSIIfITHKLREVMAIADRVTVLRRGKVVGTVDTAET-SEE 231
|
....
gi 1167959503 229 RLAE 232
Cdd:COG3845 232 ELAE 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-65 |
2.59e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 41.71 E-value: 2.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGE 65
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPEsGEILLDGQ 394
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-51 |
3.17e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 3.17e-04
10 20 30
....*....|....*....|....*....|...
gi 1167959503 19 IADLNVPLlprGKITILLGPNGCGKSTLLRSLA 51
Cdd:COG4637 13 LRDLELPL---GPLTVLIGANGSGKSNLLDALR 42
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-172 |
3.36e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.82 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 4 LMLRSFSAGYST--QPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKVVF 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEG-GQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 82 LPQSlpqgvhlhvlesiiVVLRASGGRDNAQGRAQ-----ILAILEQLGITHLALQYLDQL-----------SGGQRQLV 145
Cdd:TIGR01271 1297 IPQK--------------VFIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLM 1362
|
170 180
....*....|....*....|....*...
gi 1167959503 146 GLAQSLIRRPELLLLDEPLSALD-LNYQ 172
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-53 |
4.21e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 4.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1167959503 6 LRSFSAGYS--TQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLAGL 53
Cdd:COG2401 31 LEAFGVELRvvERYVLRDLNLEIEP-GEIVLIVGASGSGKSTLLRLLAGA 79
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-234 |
5.03e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.36 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGL-NNADGEALLDGEDLMSLSFAERAQK-VVFLPQ------------SLPQGVHLHV 94
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFyKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQhvrlfremtvieNLLVAQHQQL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 95 LESIIVVLRASGGRDNAQGRAQILAI--LEQLGITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSAL----- 167
Cdd:PRK11300 110 KTGLFSGLLKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpket 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 168 -DLNyqfHVMDLVRRDTQarnrVTI-VVAHDINIALRHGDHVLMLKDGRLVASGAPETVITAERLAEVY 234
Cdd:PRK11300 190 kELD---ELIAELRNEHN----VTVlLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
19-57 |
5.07e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.72 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1167959503 19 IADLNVPLlprGKITILLGPNGCGKSTLLRSLAGLNNAD 57
Cdd:COG4938 12 FKEAELEL---KPLTLLIGPNGSGKSTLIQALLLLLQSN 47
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
94-225 |
5.27e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 40.94 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 94 VLESIIVVLRASGGR-DNAQGRAQILAILEQLG--ITHLAlqylDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLN 170
Cdd:TIGR03269 127 VLDNVLEALEEIGYEgKEAVGRAVDLIEMVQLShrITHIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 171 YQFHVMDLVRRDTQARNRVTIVVAHDINIALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:TIGR03269 203 TAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-224 |
5.39e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLN-NADGEALLDGEDLMSLSFAERAQKV------VF-LPQSlpQGVHLHVLESIivv 101
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLITSTSKNKDIKQIrkkvglVFqFPES--QLFEETVLKDV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 102 lraSGGRDN---AQGRAQILAiLEQLGITHLALQYLDQ----LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFH 174
Cdd:PRK13649 108 ---AFGPQNfgvSQEEAEALA-REKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 175 VMDLVRRDTQarNRVTIV-VAHDINIALRHGDHVLMLKDGRLVASGAPETV 224
Cdd:PRK13649 184 LMTLFKKLHQ--SGMTIVlVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-226 |
5.92e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 2 RGLM---LRSFSAGYSTQPVIADLNVPLLPrGKITILLGPNGCGKSTLLRSLA-GLNNADGEALLDGEDLMSLSFAERAQ 77
Cdd:PRK10789 311 RGELdvnIRQFTYPQTDHPALENVNFTLKP-GQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLTKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 78 KVVFLPQSlpqgvhlHVLESIIVVLRASGGRDNAQgRAQILAIlEQLGITHLALQYLDQ------------LSGGQRQLV 145
Cdd:PRK10789 390 RLAVVSQT-------PFLFSDTVANNIALGRPDAT-QQEIEHV-ARLASVHDDILRLPQgydtevgergvmLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 146 GLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRdtQARNRVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVI 225
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQ--WGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLA 537
|
.
gi 1167959503 226 T 226
Cdd:PRK10789 538 Q 538
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-228 |
6.35e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.86 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 16 QPVIADLNVPLLPRGKITiLLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFaeraqkvvflpQSLPQGVHLhv 94
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVA-LVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSH-----------SVLRQGVAM-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 95 LESIIVVLRASG------GRDNAQgrAQILAILEQLGITHLALQYLD-----------QLSGGQRQLVGLAQSLIRRPEL 157
Cdd:PRK10790 420 VQQDPVVLADTFlanvtlGRDISE--EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167959503 158 LLLDEPLSALDLNYQ---FHVMDLVRRDTqarnrVTIVVAHDINiALRHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:PRK10790 498 LILDEATANIDSGTEqaiQQALAAVREHT-----TLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-168 |
6.48e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.79 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLmslsfaeRAQKVVFLPQSLPQGVH------LHVLESiivvL 102
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGLARPDaGEVLWQGEPI-------RRQRDEYHQDLLYLGHQpgikteLTALEN----L 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 103 RASGGRDNAQGRAQILAILEQLGIthlaLQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPLSALD 168
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVGL----AGFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-53 |
8.63e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.68 E-value: 8.63e-04
10 20
....*....|....*....|....*..
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGL 53
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-65 |
9.64e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 9.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNN-ADGEALLDGE 65
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQpQSGEILLDGK 385
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-65 |
1.08e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1167959503 27 LPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGE 65
Cdd:PRK11819 347 LPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
17-58 |
1.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.36 E-value: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1167959503 17 PVIADLNvPLLPRGKITILLGPNGCGKSTLLRSLA---GLNNADG 58
Cdd:COG3910 25 PAVRNLE-GLEFHPPVTFFVGENGSGKSTLLEAIAvaaGFNPEGG 68
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-59 |
1.55e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 4 LMLRSFSAGYSTQPVIADLNVPLLPRGKITiLLGPNGCGKSTLLRSLAG-LNNADGE 59
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIG-LLGRNGAGKSTLIKLLAGeLAPVSGE 368
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
29-92 |
1.58e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 37.57 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167959503 29 RGKITILLGPNGCGKSTLLRSLAGLNNADGEAL-LDGEDLMSLSFAERAQKVVFLPQSLPQGVHL 92
Cdd:pfam13173 1 SRKILVITGPRQVGKTTLLLQLIKELLPPENILyINLDDPRLLKLADFELLELFLELLYPGKTYL 65
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-219 |
1.90e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 39.42 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSLSFAE--RAQKVVflpqslPQGVhlhVL--ESIIVVL 102
Cdd:COG5265 382 PAGKTVAIVGPSGAGKSTLARLLFRFYDVTsGRILIDGQDIRDVTQASlrAAIGIV------PQDT---VLfnDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 103 RAsgGRDNAqGRAQIL--AILEQLG--ITHLALQYLDQ-------LSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNY 171
Cdd:COG5265 453 AY--GRPDA-SEEEVEaaARAAQIHdfIESLPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1167959503 172 QFHVMDLVRRdtQARNRVTIVVAHdinialR-----HGDHVLMLKDGRLVASG 219
Cdd:COG5265 530 ERAIQAALRE--VARGRTTLVIAH------RlstivDADEILVLEAGRIVERG 574
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
23-81 |
1.92e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 39.33 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 23 NVPLLPRGKITILLGPNGCGKSTLLRSLAGLNNADGEALLDGEDLMSLSFAERAQKV-VF 81
Cdd:COG4694 17 FGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNPSVrVF 76
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-168 |
1.97e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.39 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 13 YSTQPVIADLNVPLlPRGKITILLGPNGCGKSTLLRSLAGLNNAD-GEALLDGEDLMSlSFAERAQKVVFLPQSLPQGVH 91
Cdd:PRK13540 11 YHDQPLLQQISFHL-PAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 92 LHVLESIIVVLRASGGRdnaqgraqiLAILEQLGITHLAlQYLD----QLSGGQRQLVGLAQSLIRRPELLLLDEPLSAL 167
Cdd:PRK13540 89 LTLRENCLYDIHFSPGA---------VGITELCRLFSLE-HLIDypcgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
.
gi 1167959503 168 D 168
Cdd:PRK13540 159 D 159
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-228 |
2.03e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.74 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 14 STQPVIADLNVPLLPRGKITILlGPNGCGKSTLlrSLAGLNNAD---GEALLDGEDLMSLSFAERAQKVVFLPQSlpqgv 90
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGIC-GRTGSGKSSL--SLAFFRMVDifdGKIVIDGIDISKLPLHTLRSRLSIILQD----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 91 hlHVLESIIVVLRASGGRDNAQGR-------AQILAILEQL--GITHLALQYLDQLSGGQRQLVGLAQSLIRRPELLLLD 161
Cdd:cd03288 104 --PILFSGSIRFNLDPECKCTDDRlwealeiAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167959503 162 EPLSALDLNYQFHVMDLVRrdTQARNRVTIVVAHDINIALrHGDHVLMLKDGRLVASGAPETVITAE 228
Cdd:cd03288 182 EATASIDMATENILQKVVM--TAFADRTVVTIAHRVSTIL-DADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-51 |
2.20e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 2.20e-03
10 20 30
....*....|....*....|....*....|....*
gi 1167959503 17 PVIADLNVPLLPRGKITILLGPNGCGKSTLLRSLA 51
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG 42
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-72 |
2.67e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 2.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167959503 28 PRGKITILLGPNGCGKSTLLRSLAGLNNA-DGEALL-----DGEDL--------MSLSF 72
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTTMKMLTGLLPAsEGEAWLfgqpvDAGDIatrrrvgyMSQAF 348
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-168 |
2.69e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 38.71 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGL---NNADGEALLDGEDLMSlsfaERAQKVVFLPQSLPQGVHLHVLESIIVV----L 102
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqgNNFTGTILANNRKPTK----QILKRTGFVTQDDILYPHLTVRETLVFCsllrL 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 103 RASGGRDNAQGRAQilAILEQLGITH-----LALQYLDQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALD 168
Cdd:PLN03211 170 PKSLTKQEKILVAE--SVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
25-52 |
2.96e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.26 E-value: 2.96e-03
10 20
....*....|....*....|....*...
gi 1167959503 25 PLLpRGKITILLGPNGCGKSTLLRSLAG 52
Cdd:PRK00098 160 PLL-AGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
25-51 |
3.54e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 37.96 E-value: 3.54e-03
10 20
....*....|....*....|....*..
gi 1167959503 25 PLLPRGKITILLGPNGCGKSTLLRSLA 51
Cdd:COG3598 8 GLLPEGGVTLLAGPPGTGKSFLALQLA 34
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-200 |
3.77e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.17 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 25 PLLPRGKITILLGPNGCGKSTLLRSLAG-LNNADGEALLDGedlmslsfaeraQKVVFLPQslpqgvhlhvlesiivvlr 103
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEWDG------------ITPVYKPQ------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 104 asggrdnaqgraqilaileqlgithlalqYLDqLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDT 183
Cdd:cd03222 69 -----------------------------YID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170
....*....|....*..
gi 1167959503 184 QARNRVTIVVAHDINIA 200
Cdd:cd03222 119 EEGKKTALVVEHDLAVL 135
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-64 |
4.62e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 37.22 E-value: 4.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1167959503 30 GKITILLGPNGCGKSTLLRSLAGLNNA---DGEALLDG 64
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAgviTGEILING 70
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-148 |
6.21e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.82 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 32 ITILLGPNGCGKSTLLRSL------AGLNNADGealLDGEDLMSLSFAERAQ-KVVFlpqSLPQGVHLHVLESIIVVLRA 104
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyaltgELPPNSKG---GAHDPKLIREGEVRAQvKLAF---ENANGKKYTITRSLAILENV 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1167959503 105 sggrdnaqgraqilAILEQLGITHLALQYLDQLSGGQRQLVGLA 148
Cdd:cd03240 98 --------------IFCHQGESNWPLLDMRGRCSGGEKVLASLI 127
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
29-52 |
6.32e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 6.32e-03
|
| AAA_23 |
pfam13476 |
AAA domain; |
32-50 |
6.93e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.93e-03
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-52 |
7.13e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 37.62 E-value: 7.13e-03
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-151 |
7.46e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 32 ITILLGPNGCGKSTLLRSLA--------GLNNADGEALLDGEDLMSLSF----------AERAQK--VVFLP-------Q 84
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRyalygkarSRSKLRSDLINVGSEEASVELefehggkryrIERRQGefAEFLEakpserkE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167959503 85 SLPQGVHLHVLESIIVVLRASggRDNAQGRAQILAILEQLGITHLA----LQYLDQLSGGQRQLVGLAQSL 151
Cdd:COG0419 105 ALKRLLGLEIYEELKERLKEL--EEALESALEELAELQKLKQEILAqlsgLDPIETLSGGERLRLALADLL 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-228 |
9.73e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 37.32 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 55 NADGEALLDGEDLMSLSFAERAQKVVFLPQSlPQGVHLHVLESIivvlraSGGRDNAQ----GRAQILAILEQLgITHLA 130
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFSIVSQE-PMLFNMSIYENI------KFGKEDATredvKRACKFAAIDEF-IESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167959503 131 LQYL-------DQLSGGQRQLVGLAQSLIRRPELLLLDEPLSALDLNYQFHVMDLVRRDTQARNRVTIVVAHDInIALRH 203
Cdd:PTZ00265 1346 NKYDtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKR 1424
|
170 180 190
....*....|....*....|....*....|
gi 1167959503 204 GDHVLML----KDGRLV-ASGAPETVITAE 228
Cdd:PTZ00265 1425 SDKIVVFnnpdRTGSFVqAHGTHEELLSVQ 1454
|
|
| |
